Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин
Сигналы из окружающей среды могут восприниматься и усиливаться в клетках с помощью сигнальных каскадов. У растений фосфатидилинозитол-специфическая фосфолипаза С (ФЛС) выполняет важную роль в клеточном ответе на внешние стимулы. Субстрат и продукты ФЛС регулируют множество процессов в клетках растен...
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| Опубліковано в: : | Біополімери і клітина |
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| Дата: | 2008 |
| Автори: | , , |
| Формат: | Стаття |
| Мова: | Російська |
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Інститут молекулярної біології і генетики НАН України
2008
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| Онлайн доступ: | https://nasplib.isofts.kiev.ua/handle/123456789/157882 |
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| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин / О.М. Яковенко, С.В. Кретинін, В.С. Кравець // Біополімери і клітина. — 2008. — Т. 24, № 6. — С. 441-452. — Бібліогр.: 86 назв. — укр., англ. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraine| _version_ | 1860117585885921280 |
|---|---|
| author | Яковенко, О.М. Кретинін, С.В. Кравец, В.С. |
| author_facet | Яковенко, О.М. Кретинін, С.В. Кравец, В.С. |
| citation_txt | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин / О.М. Яковенко, С.В. Кретинін, В.С. Кравець // Біополімери і клітина. — 2008. — Т. 24, № 6. — С. 441-452. — Бібліогр.: 86 назв. — укр., англ. |
| collection | DSpace DC |
| container_title | Біополімери і клітина |
| description | Сигналы из окружающей среды могут восприниматься и усиливаться в клетках с помощью сигнальных каскадов. У растений фосфатидилинозитол-специфическая фосфолипаза С (ФЛС) выполняет важную роль в клеточном ответе на внешние стимулы. Субстрат и продукты ФЛС регулируют множество процессов в клетках растений. В настоящем обзоре мы сосредоточили внимание на молекулярных основах реализации сигнального пути фосфатидилинозитол-специфической ФЛС. Анализ данных поможет расширить представление о механизмах, лежащих в основе способности растений реагировать на разнообразные абиотические и биотические стрессы.
Сигнали довкілля можуть сприйматися та посилюватися в клітинах завдяки сигнальним каскадам. У рослин фосфатидилінозитол-специфічна фосфоліпаза С (ФЛС) виконує важливу роль у клітинній відповіді на зовнішні стимули. Субстрат та продукти цього ферменту регулюють численні процеси в клітинах рослин. В огляді зосереджено увагу на молекулярних основах реалізації сигнального шляху фосфатидилінозитол- специфічної ФЛС. Аналіз даних може доповнити уявлення про механізми, що лежать в основі здатності рослин реагувати на різноманітні абіотичні та біотичні стреси.
In plants external stimulus can be perceived and amplified in the cells by functional signaling cascades. Phosphoinositide-specific phospholipase C is an enzyme shown to initiate and provide key events in the cellular responses to extracellular signals. Both substrate and products of phospholipase C are involved in the regulation of numerous processes in plant cells. In this review, we focused on molecular basis of the phosphoinositide-specific phospholipase C signaling pathways. The data analyzed will help to elucidate the mechanisms responsible for plant’s ability to respond to a variety of biotic and abiotic stress signals.
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| first_indexed | 2025-12-07T17:36:55Z |
| format | Article |
| fulltext |
Molecular basis of phosphoinositide-specific
phospholipase C signaling pathways in plant cells
O. M. Iakovenko, S. V. Kretynin, V. S. Kravets
Institute of Bioorganic Chemistry and Petrochemistry of NAS of Ukraine
50, Kharkivske shosse, Kyiv, Ukraine, 02160
yon@bpci.kiev.ua
In plants external stimulus can be perceived and amplified in the cells by functional signaling cascades.
Phosphoinositide-specific phospholipase C is an enzyme shown to initiate and provide key events in the
cellular responses to extracellular signals. Both substrate and products of phospholipase C are involved in
the regulation of numerous processes in plant cells. In this review, we focused on molecular basis of the
phosphoinositide-specific phospholipase C signaling pathways. The data analyzed will help to elucidate the
mechanisms responsible for plant’s ability to respond to a variety of biotic and abiotic stress signals.
Keywords: phosphoinositide-specific phospholipase C, signal transduction.
In tro duc tion. Phosphoinositide-spe cific PLC (PLC) is
a key en zyme of the phosphoinositide sig nal
transduction in cells of bac te ria, pro to zoa, plants and
an i mals. It hy dro ly ses phosphatidylinositol 4,
5-biphosphate pro duc ing inositol trisphosphate and
diacylglycerol [1]. In the plant PLC plays an im por tant
role in the di ver sity of phys i o log i cal pro cesses. It is ac -
ti vated in re sponse to var i ous en vi ron men tal effectors
such as salt [2, 3], cold [4, 5], os motic stresses and
drought. More over, the plant PLC is a com po nent of
sig nal ing path ways of some phytohormones, for ex am -
ple, abscisic acid (ABA) [10, 11] and cytokinin [12].
Hav ing the unique func tions, both sub strate and
PLC prod ucts par tic i pate in the reg u la tion of nu mer ous
pro cesses [1, 13]. Inositol trisphosphate and
hexakisphosphate (inositol trisphosphate trans mu ta tion
prod uct) cause Ca2+ re lease from the intracellular stor -
age [14, 15]. Diacylglycerol can be phosphorylated by
the diacylglycerol kinase pro duc ing the lipid mes sen -
ger, phos pha tid ic acid. The ves i cle trans port in a cell is
shown to be as so ci ated closely with intracellular lo cal -
iza tion, cyclization, mo tion and deg ra da tion of pro -
teins, and reg u lated by the phospholipid mol e cules in -
clud ing phosphatidylinositol 4, 5-biphosphate and
phos pha tid ic acid [16, 1 7].
Study on PLC ac tiv ity both in vi tro and in vivo is
com pli cated by the phosphatidylinositol 4,
5-biphosphate low con tent in the higher plant or gan -
isms, and reg is tra tion of inositol trisphosphate with thin
layer chro ma tog ra phy is sel dom suc cess ful [18]. The
inositol trisphosphate anal y sis is of ten per formed with
the Amersham TRK1000 test [19]. In ves ti ga tion of
441
ISSN 1993-6842. Biopolymers and cell. 2008. vol. 24. N 6. Translated from Ukrainian
© O. M. IAKOVENKO, S. V. KRETYNIN, V. S. KRAVETS, 2008
PLC sig nal ing path ways is mostly based on ap pli ca tion
of the en zyme in hib i tors in clud ing U73122 and its in ac -
tive an a log U73343. How ever, ac cord ing to some in -
for ma tion, un der the in flu ence of U73122, the slow in -
creas ing of Ca2+ in a Ca2+-free me dium as well as block -
ing Ca2+chan nels of L-type are ob served [21]. PLC is
also stud ied us ing trans gen ic plants. The ex per i ments
on stim u la tion or de pres sion of the PLC gene ex pres -
sion, re quired to clar ify the PLC func tions in the plant
or gan isms, have been much suc cess ful [22-24]. The
study on PLC char ac ter is tics will as sist in fur ther com -
pre hen sion of the mech a nisms of phospholipid sig nal -
ing path ways con sid er ing dif fer ent as pects of plant
growth and de vel op ment.
PLC Mo lec u lar Struc ture. The five types (b, g, d,
e and f) are dis tin guished among the mam ma lian PLC.
They con tain PH-do main that is a ba sic se quence re -
quired for the at tach ment to plasma mem brane, bind -
ing with sub strate and ca tal y sis. They also have
EF-do main im por tant for the en zyme ac ti va tion, X-
and Y-se quences rep re sent ing the cat a lytic cen tre, and
C2-do main en sur ing in ter ac tion with Ca2+ and lipids
[25, 26]. Such struc ture is typ i cal for PLC d-isoform
while there are ad di tional do mains in other PLC fam i -
lies. The plant PLC is struc tur ally iden ti cal to the
small est mam ma lian PLC z-isoform of about 60-70
kD, which has two EF-hand se quences, X-, Y-, and
C2-do mains but not the PH-do main typ i cal for the
other PLC isoforms [27].
How ever, it should be noted that on the se quence
level PLC is closer to the mam ma lian PLC d-isoform
[28, 29]. The plant PLC does not con tain PH-do main,
which is nec es sary for the in ter ac tion of the an i mal PLC
with plasma mem branes. PLC con tains
C2-Ca2+/phospholipids -bind ing do main fix ing the cat -
a lytic cen tre in cor rect po si tion. This do main par tic i -
pates in the in ter ac tion with mem brane but its pres ence
is not suf fi cient for the en zyme to form cat a lyt i cally ac -
tive state and other PLC do mains are re quired to
associate with plasma membranes [26, 30].
PLC Genes Ex pres sion and Evo lu tion. For the
first time, DNA en cod ing for PLC was iden ti fied in an i -
mal cells in 1988 [31]. Seven years later the
Arabidopsis thaliana L. [2] and soy bean (Glycine max
L.) PLCs were cloned and the pres ence of this en zyme
pro tein was dem on strated in both plasma mem brane
and cytosol [32]. Now a days, a lot of the ac tive PLC
cod ing genes are known and the PLC pro teins were ob -
tained from cer tain plants, for ex am ple, po tato
(Solanum tuberosum L.) [33], mungbean (Vigna
radiata L.), maise (Zea mays L.), rice (Oryza sativa L.)
[1], and pe tu nia (Pe tu nia inflata L.) [30].
In the A. thaliana ge nome there are 9 AtPLC genes
[22, 29]. AtPLC1 - AtPLC5 genes en code for PLC the ac -
tiv ity of which was proved in vi tro, whereas the en zy -
matic ac tiv ity of AtPLC8 and AtPLC9 prod ucts is hardly
prob a ble [22, 34]. AtPLC6 and AtPLC7 con tain the do -
main re quired for the PLC ac tiv ity and en code the ac tive
en zyme. Pre vi ously it was es tab lished that AtPLC7 en -
codes in com plete and non-func tional pro tein with mo -
lec u lar mass of 30 KD [22]. How ever, sub se quently
there was dis cov ered the full-chain AtPLC7 DNA, prob -
a bly en cod ing the PLC func tional pro tein [35].
The cat a lytic do mains of all PLCs have the sim i lar
struc ture and ox i da tion-re duc tion ca tal y sis mech a nism.
The con ser va tism of to pol ogy and el e ments of the ac -
tive site in di cate their or i gin from a sin gle al lied pro -
tein. The phylo gen etic his tory of eukaryotic PLC prob -
a bly in cludes sev eral stages of chain elon ga tion and
gene du pli ca tion. The AtPLC gene fam ily evo lu tion
seems to go through sev eral phases. The gene tan dem of
AtPLC8 and AtPLC9 arose due to the lo cal du pli ca tion
on later stages. AtPLC1, AtPLC4 and AtPLC5 make up
a group of genes com bined from small DNA frag ments.
Prob a bly, the pre cur sor of AtPLC4/AtPLC5 and
AtPLC1/AtPLC3 arose from a sin gle gene dur ing the
du pli ca tion in the 5th chro mo some with the fur ther
AtPLC3 du pli ca tion and translocation onto the 4th
chromosome responsible for the further gene
distribution [35].
The ex pres sion of AtPLC gene in creases in re -
sponse to such en vi ron men tal fac tors as de hy dra tion,
salinization and cold stress [2, 36]. The po tato PLC
genes are ex pressed in re sponse to the wound ing stress
and wa ter deficit [33].
The AtPLC1 and AtPLC6 tran scrip tion is in duced
in re sponse to some abiotical stresses in clud ing de hy -
dra tion, sa lin ity and cold stress [2, 34] (see the ta ble).
The tran scrip tion level in cre ment is sup posed to re sult
in the AtPLC pro tein in crease and thereby it ac ti vates
the sig nal ing path ways of up- or down-reg u la tion of
genes par tic i pat ing in var i ous cell re ac tions. For ex am -
442
IAKOVENKO O. M., KRETYNIN S. V., KRAVETS V. S.
ple, the AtPLC1 tran scrip tion, the en zyme ac ti va tion
and in crease in the inositol trisphosphate level were
dem on strated to be re quired for the fur ther gene ex pres -
sion in response to the abscisic acid influence.
AtPLC1 is ac ti vated in re sponse to the in flu ence of
salt, abscisic acid, cold and de hy dra tion. The AtPLC2
gene ex pres sion is not in duced un der the in flu ence of
abiotical stresses [37]. Un like the AtPLC2, the other 8
genes of AtPLC are in duced in re sponse to the ex ter nal
in flu ence. For AtPLC8 and AtPLC9 the tran scrip tion
level in creases less than two fold un der the in flu ence of
all ex ter nal stim uli [35]. (More than two-fold in ten si fi -
ca tion of) The AtPLC6 in duc tion rise more than two -
fold was dem on strated as a re sult of ac tion of some ex -
ter nal fac tors [2].
The phys i o log i cal role of PLC in the re sponse of
plants to the abiotic stress was de scribed us ing the
trans gen ic maize. The abiotic stress does not change ei -
ther the wild phe no type or the phe no type of plants with
de pressed or height ened PLC gene ex pres sion which
were grown in the op ti mal con di tions. How ever, un der
the in flu ence of wa ter stress the plants with di min ished
PLC1 ex pres sion dif fered by a low wa ter con tent in tis -
sues, osmoregulation de te ri o ra tion, photosynthetic ac -
tiv ity de cay, high per cent age of ion loss, higher lipid
peroxidation in ten sity and lesser pro duc tiv ity in com -
443
BASIS OF PHOSPHOLIPASE C SIGNALING PATHWAYS IN PLANT CELLS
Influence Activated isoform Object Literature source
Abscisic acid AtPLC6 Arabidopsis thaliana L. [34]
TfPLC2 Torenia fournieri L. [85]
AtPLC1–9, êðîìå AtPLC2 A. thaliana L. [35]
Decrease of the temperature AtPLC1 A. thaliana L. [2]
AtPLC1–5 A. thaliana L. [22]
BnPLC2 Brassica napus L. [9]
ZmPLC Zea mays L. [86]
AtPLC1–9, êðîìå AtPLC2 A. thaliana L. [35]
Increase of the temperature AtPLC6 A. thaliana L. [34]
Salt stress AtPLC1 A. thaliana L. [2]
AtPLC1–5 A. thaliana L. [22]
AtPLC6 A. thaliana L. [34]
VrPLC3 Vigna radiata L. [7]
ZmPLC Z. mays L. [86]
ZmPLC1 Z. mays L. [38]
De hy dra tion AtPLC1 A. thaliana L. [2]
StPLC1 Solanum tuberosum L. [33]
AtPLC1–5 A. thaliana L. [22]
VrPLC3 V. radiata L. [7]
ZmPLC Z. mays L. [86]
TfPLC2 T. fournieri L. [85]
Enhancement of phosphatydylinositol specific phospholipase C expression in plant cells in response to abiotic factors and influence of
abscisic acid.
par i son with the wild. There was drawn a con clu sion on
fail ure of sig nal transduction mech a nism and, be cause
of this, in abil ity of cells of pro vid ing the ad ap ta tion to
the stress which in di cates the es sen tial role of PLC
genes in the regulation of response to the stress caused
by water deficit [38].
PLC Ki netic Prop er ties. Most of the ac tive plant’s
PLCs were ob tained from cytosol, but as the sub strate
of this en zyme is as so ci ated with mem brane the en zyme
ac tiv ity in cytosol and mem branes may dif fer. Be cause
of this one of the most in ter est ing tasks is to study the
ac ti va tion of PLC on the mem brane sur face. The PLC
ac tiv ity in Catharanthus roseus L was de scribed us ing
the lipid sub strates, dis trib uted in the phospholipid ves -
i cles, phospholipid mi celles and monolayer in the
air-wa ter me dium [39]. The ap pli ca tion of P33-la beled
sub strate for the di rect mea sure ment of the
Catharanthus roseus L. PLC ac tiv ity re vealed de pend -
ence of the monolayer PC-PS pro por tion and amount
on the pres sure. The PLC ac tiv ity in creases when the
pres sure is raised up to 20 mN/m2 and reaches the max i -
mum un der these con di tions. The fur ther pres sur iza tion
leads to the PLÑ ac tiv ity de cay. Prob a bly, the PLC ac -
tiv ity re duc tion is caused by de crease in the en zyme
abil ity to bind the sub strate. This phe nom e non is spe -
cific and seems to de pend on the phosphatidylinositol
4, 5-biphosphate con cen tra tion. These re sults dif fer
from those re ceived for the an i mal d-PLC and are sim i -
lar to b-PLC. This is un ex pected be cause struc tur ally
the plant PLC is closer to the d-PLC isoform. How -
ever, it was dem on strated that the d-PLC isoform ac -
tiv ity de creases lin early at in creas ing sur face pres sure.
What is the rea son of the dif fer ences be tween the ac -
tiv i ties of the plant PLC and d-PLC in a monolayer is
un known, but the de pend ence of dif fer ent isoforms
ac tiv ity on the char ac ter is tics of the sur faces which
they in ter act with was de ter mined. Thus, as a re sult of
study ing the PLC of plants and other or gan isms [40,
41] it was es tab lished that the phosphatidylinositol
4,5-biphosphate hy dro ly sis in a monolayer de pended
on the sur face pres sure de ter min ing the pe cu liar i ties
of in ter ac tion be tween the en zymes of this fam ily and
the lipid sur face [39].
This in for ma tion and the re sults, ob tained us ing the
monolayer sub strate where the PLC ac tiv ity de creased
as the sub strate pres sure in creased, in di cate that PLC
has to pen e trate through the lipid ag gre gates in the case
of the sub strates bind ing and hy dro ly sis. The data on
ve sic u lar bind ing con firms the plant PLC in ter ac tion
with the mem brane sur face by the phosphatidylinositol
4, 5-biphosphate sub strate. To pro vide the for ma tion of
the PLC-me di ated sec ond ary mes sen gers PLC can in -
ter act with the mem brane sur face in spe cific non-cat a -
lytic way with fur ther bind ing or sur face re or ga ni za -
tion. This can pro mote a sta ble fix a tion of PLC on the
mem brane sur face [42].
The un ex pected re sults were re ceived dur ing in ves -
ti ga tion of the sur face in ter act ing site and fur ther bind -
ing of the lipid sub strate in side the mem brane. Prob a -
bly, the Mi chae lis-Menten equa tion curve with Hill co -
ef fi cient close to 1 in di cates the ex is tence of a sin gle
bind ing site. The an i mal PLC amino-ter mi nal re gion,
con tain ing pleckstrin ho mol o gous do main, is nec es sary
for bind ing with phospholipid ves i cles which con tain
phosphatidylinositol 4, 5-biphosphate. These re sults
con firm that the pres ence of phosphatidylinositol 4,
5-biphosphate can be an im por tant fac tor, re quired for
the lo cal iza tion of the pro teins, which con tain this do -
main on the mem brane sur face. How ever, the pleckstrin
ho mol o gous do main has not been re vealed among the
prod ucts of the plant PLC genes. Per haps, the plant
PLC ini tially has to af fil i ate with phosphatidylinositol
4, 5-biphosphate in the catalytic site n [43].
The en an tio mer pure an a logues of all nat u ral PLC
sub strates, in clud ing both long- and short-chain
phosphatidylinositol 4, 5-biphosphates, phos pha tid yl-
inositol 5-phos phates and non-phosphorylated
phosphatidylinositols, were syn the sised. The sub strates
phosphorylated at the 4-inositol bond
(phosphatidylinositol 4, 5-biphosphate and
phosphatidylinositol 5-phos phate) have very sim i lar ki -
netic prop er ties and their phosphorylation pro gresses
20-30 times more ac tively than those non-phospho-
rylated (phosphatidylinositol 4-phos phate and
phosphoinositide). So it can be con cluded that the in ter -
ac tion ex actly with the 4-phos phate group is re quired
for the PLC ca tal y sis. Fur ther more, the bind ing af fin ity
of all four groups is rather sim i lar that in di cates the en -
ergy suf fi ciency of en zy matic bind ing with the
4-phosphate group for the catalysis.
The spec i fic ity of the wheat root PLC to wards the
polyphosphoinositides de pends on the var i ous fac tors:
444
IAKOVENKO O. M., KRETYNIN S. V., KRAVETS V. S.
pH (pH 6-7 - the phosphoinositide-phos phate hy dro ly -
sis, pH 6-6.5 - phosphoinositide 4, 5-biphosphate hy -
dro ly sis) and (kind of the) ions. The cal cium, man ga -
nese and co balt ions at the con cen tra tion of 4 mM di -
min ish the PLC spec i fic ity to wards
phosphoinositide-biphosphate and in ten sify the
phosphoinositide-phos phate hy dro ly sis. At high cal -
cium con cen tra tion the PLC spec i fic ity changes in such
row: phosphoinositide > phosphoinositide-4-phos phate
> phosphoinositide 4, 5-biphosphate [45].
PLC can be di vided into 2 groups by the in vi tro
prop er ties: sol u ble forms which are spe cific to wards
phosphoinositide and re quire cal cium of mM con cen tra -
tions for ca tal y sis, and PLCs, at tached to the
plasmalemma with a sub strate spec i fic ity to wards the
polyphosphoinositides, re quir ing µM con cen tra tions of
cal cium for ac ti va tion (the op ti mum is 0.1-10 µM) [30].
The pu ri fied mem brane PLC is highly spe cific to wards
phos phates (100% ac tiv ity); crude en zyme is more spe -
cific to wards the polyphosphoinositides (10% ac tiv ity
for phosphoinositide-phos phate and 30% for
phosphoinositide-4, 5—biphosphate). The ac tiv ity of
pu ri fied form to wards phosphoinositide 4,
5-biphosphate is re stored by ad di tion of a pro tein lost
dur ing the en zyme pu ri fi ca tion. How ever, it was dem on -
strated that this reg u la tory fac tor is not a G-pro tein [45].
Reg u la tion of PLC ac tiv ity. G-pro teins.
Heterotrimeric G-pro tein con sists of a-, b- and g-sub -
units and op er ates as a mo lec u lar switch con trol ling a
great num ber of cel lu lar re ac tions, trans mit ting the sig -
nal from the cell sur face re cep tors to the intracellular
eliñitors, such as PLC, phospholipase D, cyclases, ion
chan nels, phosphodiesterases, etc. [46]. In the hu man
ge nome there are about 1000 genes for G-pro teins,
whereas in the A. thaliana ge nome only one gene of
G-pro tein, par tic i pat ing in the cell cy cle reg u la tion [47]
and abscisic acid sig nal ing in the guard cells [48], has
been found up to now. A G-pro tein was dem on strated
to par tic i pate in the ion chan nel reg u la tion [49] and cel -
lu lar pro lif er a tion of the A. thaliana plants [50]. More -
over, the mu ta tions in the A. thaliana and rice G-pro -
tein re sult in the dam age of a wide range of pro cesses,
such as seed germination, spear and root growth, stoma
movement [50].
Three le gumes G-pro tein sub units were ob tained
and de scribed; G-pro tein par tic i pa tion in the salt and
ther mal stress sig nal transduction, and the in ter ac tion
be tween G-pro tein and PLC were dem on strated. The
in ter ac tion be tween the G-pro tein a-sub unit is an im -
por tant stage of salinization sig nal transduction. The
thermotolerance is based on the Gb-me di ated sig nal
transduction. A fur ther study is re quired to clar ify the
reg u la tion of these pro teins in re sponse to the salt and
ther mal stresses, and to un der stand their role in the
adaptation [51].
The change in inositol trisphosphate con cen tra tion
is ob served in re sponse to an in crease in the ty ro sine
kinase ac tiv ity and PLC ac ti va tion dur ing the G-pro tein
ac ti va tion at in fec tion of Cit rus limon L. le sion with
Altemaria al ter nate fun gus. It was es tab lished that two
sig nal path ways are ac ti vated: one – with par tic i pa tion
of G-pro tein, an other - with ty ro sine kinase-de pend ent
PLC. A pos si bil ity of the re la tion be tween PLC ac ti va -
tion and ty ro sine kinases requires fur ther research [52].
The reg u la tion of PLC ac tiv ity by cal cium ions.
Cal cium is a main ac ti va tor among the ions able to in -
flu ence the PLC ac tiv ity. The op ti mum cal cium con -
cen tra tion for the PLC ac tiv ity in microsome frac tions
and plasma mem branes of Bras sica napus cells is
10-5-10-4 M [53].
The max i mum phosphoinositide 4, 5-biphosphate
hy dro ly sis by the soya PLC is ob served at pH op ti mum
of 6.5-7.5 [54]. The lipid hy dro ly sis by the po tato PLC
in ten si fied at the cal cium con cen tra tion of 100 µM. The
spec i fic ity of PLC 1 to wards phosphoinositide 4,
5-biphosphate starts to di min ish at more than 100 µM
cal cium, whereas PLC 2 and PLC 3 lose the spec i fic ity at
a higher cal cium con cen tra tion of 100-10000 µM [33].
The A. thaliana PLC 1 in hi bi tion does not de press
the Cor and RD29a stress genes ex pres sion in duced by
the abscisic acid [20]. Per haps, the syn the sis of the cy -
clic ADP-ribose will me di ate the ini tial cytosolic cal -
cium con cen tra tion rise re sult ing in the PLC ac ti va tion.
How ever, this does not rule out the pos si bil ity that other
isoforms of PLC can ini ti ate si mul ta neously a pri mary
re sponse and a cal cium flux into the cell even at low
cal cium con cen tra tions. At least one of the A. thaliana
PLC isoforms, namely AtPLC4, is ac tive in the absence
of calcium [22].
AtPLC1 mainly hy dro ly ses phosphoinositide
4,5-biphosphate. At the op ti mum cal cium con cen tra -
tion phosphoinositide 4, 5-biphosphate is hy dro lyzed
445
BASIS OF PHOSPHOLIPASE C SIGNALING PATHWAYS IN PLANT CELLS
by 100 times more ef fi ciently than phosphoinositide.
The max i mum hy dro ly sis is ob served at 1-50 µM cal -
cium, and at the cal cium con cen tra tion of more than 1
mM the phosphoinositide hy dro ly sis pre vails (like the
po tato and soya PLC). The Mi chae lis-Menten con stant
for the PLC of C. roses roots is 0.0518 and the sub strate
con stant is 45.5µM, the max i mum re ac tion rate is 137.2
picomoles/min [39].
A need for Ca2+ for the ac ti va tion of many plant
PLC seem to in di cate that inositol trisphosphate for ma -
tion is not a pri mary re sponse to the stress since the Ca2+
level rise is first re quired for the PLC ac ti va tion and
phosphoinositide for ma tion. The cal cium level can in -
crease due to the cal cium flux from ex tra cel lu lar me -
dium or be cause of the ac tion of sec ond ary mes sen gers
able to re lease Ca2+, e.g. cy clic ADP-ribose [56, 57],
nic o tinic acid adeninedinucleotidphosphate [58],
sphingosin-1-phos phate [59], hy dro gen per ox ide [60],
and hexakisphosphate [61].
The study on reg u la tion of five AtPLC isoforms by
cal cium dem on strated that A. thaliana PLC 2 is the
most sus cep ti ble to the cal cium ion ef fect: at the con -
cen tra tion of 10 nM its ac tiv ity was 80% of max i mum.
The sus cep ti bil ity to the µM cal cium con cen tra tions di -
min ishes in the fol low ing or der: PLC4 - PLC5 - PLC1.
PLC 3 has the weak est re sponse to cal cium: at 10 nM
con cen tra tion the ac tiv ity is 15% of max i mum. PLC4 is
the most sta ble at low cal cium level - its ac tiv ity is 20%
of max i mum in the pres ence of EGTA. All A. thaliana
PLCs ex cept for PLC 3 are the most ac tive at the cal -
cium con cen tra tion of 3 µM and pre serve their ac tiv ity
on the same level at the cal cium con cen tra tion of 10
µM. In case of mi cro mo lar cal cium con cen tra tions the
PLC isoform ac tiv i ties dif fer. PLC 2, PLC 4 and PLC 5
reach the max i mum ac tiv ity level at the cal cium con -
cen tra tion of 1µM whereas PLC1 and PLC3 re quire
higher cal cium con cen tra tions for the max i mum ac tiv -
ity. The over lap ping of the A. thaliana var i ous PLC
genes ex pres sion in di cates their func tional ex cess.
How ever, it is also pos si ble that the reg u la tion of each
gene and PLC is ex erted in dif fer ent ways. The cal cium
re lease un der the in flu ence of one of the PLC isoforms
can cause an ac ti va tion of the oth ers. The per ma nent ex -
pres sion of A. thaliana PLC2 and PLC3 ev i dences for
their par tic i pa tion in the pri mary re sponse to a stress,
caus ing the cal cium ion concentration rise to induce the
PLC1, PLC4 and PLC4 genes expression along with
other genes ac ti vated by calcium [22].
The Mo lec u lar Mech a nisms of PLC Sig nal Path -
way Re al iza tion in the Plant Cells. Inositol
triphosphate, hexakisphosphate. The inositol
trisphosphate ad min is tra tion into the cells re sults in the
cy to plas mic cal cium con cen tra tion rise, stomata clos -
ing, proto plasts swell ing, fer til iza tion tube growth in hi -
bi tion, and plasmodesma clos ing [62]. Inositol
trisphosphate is a sec ond ary mes sen ger which re lease
cal cium out of the intracellular de pot in plant cells [14].
High-af fin ity sites for inositol trisphosphate bind ing in
an i mals are lo cated on the endoplasmic re tic u lum (ER).
An as sumed inositol trisphosphate re cep tor was ob -
tained from the Vigna ra di ate L and char ac ter ised. In
com par i son with the an i mal cell re cep tors it is smaller
(110 against 250 kD), and its ac tiv ity is in ten si fied by
the inositol phos phate me tab o lites [63]. The ex is tence
of the cal cium chan nels sen si tive to inositol
trisphosphate on the non-vacuolar mem branes was
proved. How ever, up to now the at tempt to ex tract the
inositol triphosphate-reg u lated chan nel pro tein has
failed. The inositol trisphosphate re cep tors genes ho -
mol o gous to the an i mal ones also have not been found
in the A. thaliana ge nome [64]. In the plants
Chenopodium rubrum L. the inositol trisphosphate
bind ing sites are lo cated on the ER [54]. It was dem on -
strated that the inositide-2, 4, 5-trisphosphate stim u -
lates cal cium re lease from the intracellular de pot rather
ef fi ciently, but slighter than inositide-1, 4,
5-trisphosphate [65]. Per haps, the inositol
triphosphate-phytase com plex in ter acts with the
inositol trisphosphate re cep tors re sult ing in cal cium re -
lease from the microsome frac tions whereas
inotitide-1,3,4-trisphosphate does not have such ca pa -
bil ity since it does not bind to the re cep tors [65]. Study
in vi tro on the Chenopodium Rubrum L .plants re vealed
the in ter ac tion of inositol triphosphate-phytase with the
inositol trisphosphate re cep tors, which re quires the
nanomolar con cen tra tion of the sub strate. The inositol
trisphosphate bind ing with a highly af fine non-cat a lytic
site of the phytase re sults in the es sen tial con for ma tion
changes in the en zyme. This causes the for ma tion of
inositol triphosphate-phytase-re cep tor com plex with
much more ac tive re lease of cal cium com par ing to free
inositol trisphosphate [63]. These in ves ti ga tions are in
446
IAKOVENKO O. M., KRETYNIN S. V., KRAVETS V. S.
fa vour of the ex is tence of a new signal cascade,
regulating the calcium homeostasis, which is mediated
by the hexakisphosphate-phytase system in the plant
cells [65].
A role of hexakisphosphate is not stud ied enough.
The S. tuberosum L. and V. faba L. stomata cells treat -
ment with abscisic acid in creases the level. The
hexakisphosphate was shown to screen the in hib it ing
ef fect of abscisic acid and cal cium on the po tas sium
chan nels [15]. The hexakisphosphate and phos pha tid ic
acid, formed in the yeast from inositol trisphosphate
and diacylglycerol, reg u late the gene tran scrip tion and
mRNA trans port [66]. This ex plains the ab sence of the
genes, cod ing the cal cium chan nels which are reg u lated
by inositol triphosphate, and the ab sence of the pro tein
kinase C genes in the genome of these organisms.
The inositol trisphosphate level is strictly reg u lated.
The plant inositol phosphatases dif fer sig nif i cantly
from the an i mal ones. For the pants it was es tab lished in
vivo [18] and in vi tro [67] that the inositol-1, 4,
5-trisphosphate is hy dro lysed by the en zymes
inositol-polyphosphate-1’-phosphatase and
inositol-polyphosphate-5’-phosphatase, to pro duce
inositide-4, 5-biphosphate and inositide-1,
4-biphosphate.
Diacylglycerol, diacylglcerolpyrophosphate, phos -
pha tid ic acid. The in crease in DAG level stim u lates the
H+-ATP-ac tiv ity and the stomata open ing, af fects cell
di vi sion, ham pers the pro tein move ment through the
plasmodesma and in ten si fies the phosphorylation [67].
The cell treat ment with DAG in vivo re sults in the
change of cytoskeleton flex i bil ity the re duc tion of
intervacuolar fil a ment ten sion. DAG is also in volved
into the pro cess of mi to sis in the cells of sta men fil a -
ments. Fur ther more, DAG in duces the ion ab sorp tion in
the iso lated proto plasts of guard cells and stomata
open ing [62]. How ever, it is not es tab lished whether
these ef fects are caused di rectly by DAG or its me tab o -
lites (for ex am ple, fatty ac ids and phos pha tid ic acid
(PA)). Most of the ob ser va tions in di cate the DAG
phosphorylation im me di ately af ter its for ma tion [62,
69, and 70].
The phos pha tid ic acid rise was dis cov ered in var i -
ous types of the plant cells un der the in flu ence of the os -
motic stress, wound, patho gens, abscisic acid, ox i da -
tive stress, Nod-fac tors, and drought [70]. The for ma -
tion of 18:3/16:3- PA through the DAG phosphorylated
by the DAG kinase was ob served un der the freez ing
and in flu ence of the patho gens. The phospholipase D is
also an im por tant PA generator [1, 24].
There was dis cov ered a lot of pro teins able to bind
with PA, for ex am ple, MARK [3] and protonic ATP
[6], pro tein kinase in flu enc ing the actin poly meri sa -
tion [71], NADPH-oxidase [72], pro tein kinase de -
pend ent on cal cium [73], SNF-bound pro tein kinase
SnRK2.10, reg u la tive sub unit of 2A pro tein
phosphatase RCN1, DRG1, spe cific isoforms of the
14-3-3 pro tein GRF6 (l) and GRF8 (k), heat-shock
pro tein isoforms, sev eral tubulin isoforms, and the
isoforms of phospho- enolpyruvate carboxylase (Ppc1
and Ppc3) [17, 71].
The PA sig nal ling is al ways im pet u ous and tran -
sient that is en sured by the sig nal de pres sion mech a -
nism [70]. The res to ra tion of the ini tial con cen tra tion
is very im por tant for most of the sig nal mol e cules. In
the plant cells the PA sig nal ling weak ens due to its
phosphorylation by PA kinase with pro duc ing
diacylglcerolpyrophosphate (DGPF) [62, 70]. At rest
the DGPF con cen tra tion in cells is very low, and the
ex pres sion level of PA kinase, which is re spon si ble for
DGFP for ma tion, re mains con stant for all plants. This
stip u lates a close as so ci a tion be tween the DGPF for -
ma tion and its pre cur sor PA avail abil ity. Since the
DGPF for ma tion co in cides with PA level low er ing,
the PA kinase can take part in the PA sig nals de pres -
sion. In vivo the PA kinase ac ti va tion was dis cov ered
in yeast and in many plant sys tems in re sponse to the
var i ous phys i o log i cal stim uli, in clud ing his hy per os -
motic stress, drought and patho gens at tack. Thus, a
pos si ble role of DGPF as a sec ond ary me di a tor for
PLC sig nal trans- duction in the plant cells should not
be ex cluded [70].
The Phosphatidylinositol 4, 5-biphosphate
Func tions in the Plant Cells. In the an i mal cells
phosphatidylinositol 4, 5-biphosphate is not only a sub -
strate of PLC, but it can be also a sig nal ing mol e cule in -
flu enc ing var i ous bi o log i cal pro cesses in cells [13]. The
phosphatidylinositol 4, 5-biphosphate of higher plants is
a reg u la tor of the sig nal path ways. The change in
intracellular phosphatidylinositol 4, 5-biphosphate level
is ob served in re sponse to the in flu ence of light, cold,
grav i ta tional stim u la tion, ox i da tive stress, G-pro teins ac -
447
BASIS OF PHOSPHOLIPASE C SIGNALING PATHWAYS IN PLANT CELLS
ti va tion, and patho genic elicitors [74]. Pos si ble pro -
cesses with phosphatidylinositol 4, 5-biphosphate as sis -
tance are listed here un der:
1. Ion chan nels reg u la tion. Phosphatidylinositol 4,
5-biphosphate is con sid ered to be a key reg u la tor of ion
chan nels ac tiv ity, es pe cially K+ [75]. The
phosphatidylinositol 4, 5-biphosphate ac cu mu la tion in
the plant plasma mem brane in duced by the salt stress
can re flect this func tion [13].
2. Mem branes for ma tion and flu id ity. Dur ing the
mam ma lian cell di vi sion phosphatidylinositol 4,
5-biphosphate is mainly lo cal ized in the mem brane and
is re quired for the cytokinesis ac com plish ment for the
ac tive area for ma tion, ef fec tive mem brane fu sion, and
cell division [76, 77].
3. The cytoskeleton re or gani sa tion.
Phosphatidylinositol 4, 5-biphosphate is in volved into
the cleav age fur row for ma tion. It is bound with
actin-reg u la tory pro teins and can in flu ence their ac tiv -
ity [78, 79, and 80]. More over, an in crease in the lo cal
phosphatidylinositol 4, 5-biphosphate level can pro -
mote pro teins in ter ac tion with the plasma mem brane
hav ing spe cific phosphatidylinositol 4,5-biphosphate-
bind ing sites [79, 81]. The plants are sup posed to con -
tain sev eral such do mains in clud ing the cytoskeleton
or gan is ing pro teins [1, 13]. The low phos pha tid yl-
inositol 4, 5-biphosphate level in plants can be ex -
plained by ei ther a higher af fin ity of the plant pro tein
do mains to wards lipids com pared with the mam ma -
lian ones, or the af fin ity of com ple men tary pro tein do -
mains to wards the other com po nents, which are nec es -
sary for ef fi cient bind ing with the plasma mem brane.
The con fir ma tion of such func tions may be the re -
sponse ob served dur ing cell di vi sion and salt stress as
well as changes in the cy to plas mic re tic u lum, in duced
by U71322, and an in flu ence on the vac u oles mor -
phol ogy [13]. The phosphatidylinositol 4,
5-biphosphate par tic i pa tion in actin cytoskeleton reg -
u la tion was also dem on strated dur ing the fer til iza tion
tube growth [30].
4. The mem brane trans por ta tion. In the mam ma lian
cells a lot of polyphosphoinositides are in volved into
the exocytosis and/or endocytosis [79, 82]. How ever,
the phosphatidylinositol 4, 5-biphosphate ac cu mu la -
tion in small ves i cle struc tures is not ob served [84]. The
phosphatidylinositol 4, 5-biphosphate po lar gra di ent
can re flect the mem brane trans por ta tion events dur ing
the root fi brils growth [30, 84].
De spite the va ri ety of PLC sig nal ling mech a nisms,
a mi nor quan tity of phosphatidylinositol 4,
5-biphosphate pres ent in the mem branes of higher
plants is reg is tered on the re cently formed mem branes
of the di vid ing cells, ac cu mu lat ing in the mem branes in
re sponse to the salt stress [13]. The de crease in
phosphatidylinositol 4, 5-biphosphate level in the
stomata guard cells in re sponse to the abscisic acid in -
flu ence in di cates its par tic i pa tion in the abscisic acid
sig nal ling cas cades, ac ti vat ing the stomata clos ing [55].
It was dem on strated that the phosphatidylinositol
4,5-biphosphate-bind ing pro tein in hib its the stomata
open ing in duced by light, re sult ing in re duc tion of the
free phosphatidylinositol 4,5-biphosphate level de -
crease in the inositol trisphosphate and phos pha tid ic
acid for ma tion un der the in flu ence of PLC and D; be -
sides, it stops the stomata clos ing caused by abscisic
acid [74]. Light-de pend ent in cre ment of
phosphatidylinositol 4,5-biphosphate con tent in the
plasma mem brane can oc cur not only due to in creas ing
syn the sis but also be cause of re duc tion of
phosphatidylinositol 4,5-biphosphate hy dro ly sis by
PLC. The di min ished PLC ex pres sion re duces the in hib -
i tory ef fect of abscisic acid on the seed ger mi na tion and
the in flu ence of this phytohormone on the ex pres sion of
the drought- and cold- re spon sive genes [37].
PLC plays a sig nif i cant role in the abscisic acid sig -
nal transduction in the stomata guard cells. U73122 (a
PLC in hib i tor) re duces the guard cells re sponse to the
abscisic acid ac tion and Ca2+ fluc tu a tions in cytosol
[11]. More over, a de crease in the PLC level in the
stomata guard cells par tially pre vents the in hi bi tion of
stomata open ing by abscisic acid [22, 23]. U73122 was
used to study PLC in the light-in duced stomata open ing
.The stomata guard cells af ter the in hib i tor treat ment
speed up the open ing caused by cir ca dian rhythm. The
ques tion whether the PLC reg u la tion of the re sponse to
the light in flu ence oc curs in the same way as the
abscisic acid sig nal ling, still re mains open [74].
Thus, de spite the re cent sig nif i cant achieve ments in
the study on the PLC ki net ics, gene ex pres sion and par -
tic i pa tion of this en zyme in the cell sig nal cas cades, the
mech a nisms of reali sa tion of PLC-me di ated sig nal ling
path way re quire fur ther in ten sive many-sided research.
448
IAKOVENKO O. M., KRETYNIN S. V., KRAVETS V. S.
The work was sup ported by the Ukrai nian Foun da -
tion for Fun da men tal re search, grant F14.4/253-2007.
Î. Í. ßêî âåí êî, Ñ. Â. Êðå òè íèí, Â. Ñ. Êðà âåö
Ìî ëå êó ëÿð íûå îñíî âû ðå à ëè çà öèè ñèã íàëü íî ãî ïóòè ôîñ ôà òè -
äè ëè íî çè òîë-ñïå öè ôè ÷åñ êîé ôîñ ôî ëè ïà çû Ñ â êëåò êàõ ðàñ òå -
íèé
Ðå çþ ìå
Ñèã íà ëû èç îêðó æà þ ùåé ñðå äû ìî ãóò âîñ ïðè íè ìàòü ñÿ è óñè -
ëè âàòü ñÿ â êëåò êàõ ñ ïî ìîùüþ ñèã íàëü íûõ êàñ êà äîâ. Ó ðàñ òå -
íèé ôîñ ôà òè äè ëè íî çè òîë-ñïå öè ôè ÷åñ êàÿ ôîñ ôî ëè ïà çà Ñ
(ÔËÑ) âû ïîë íÿ åò âàæ íóþ ðîëü â êëå òî÷ íîì îò âå òå íà âíåø -
íèå ñòè ìó ëû. Ñó áñòðàò è ïðî äóê òû ÔËÑ ðå ãó ëè ðó þò ìíî -
æåñ òâî ïðî öåñ ñîâ â êëåò êàõ ðàñ òå íèé. Â íà ñòî ÿ ùåì îá çî ðå
ìû ñî ñðå äî òî ÷è ëè âíè ìà íèå íà ìî ëå êó ëÿð íûõ îñíî âàõ ðå à ëè çà -
öèè ñèã íàëü íî ãî ïóòè ôîñ ôà òè äè ëè íî çè òîë-ñïå öè ôè ÷åñ êîé
ÔËÑ. Àíàëèç äàí íûõ ïî ìî æåò ðàñ øè ðèòü ïðåä ñòàâ ëå íèå î
ìå õà íèç ìàõ, ëå æà ùèõ â îñíî âå ñïî ñîá íîñ òè ðàñ òå íèé ðå à ãè -
ðî âàòü íà ðàç íî îá ðàç íûå àáè î òè ÷åñ êèå è áè î òè ÷åñ êèå ñòðåñ -
ñû.
Êëþ ÷å âûå ñëî âà: ôîñ ôà òè äè ëè íî çè òîë-ñïå öè ôè ÷åñ êàÿ
ôîñ ôî ëè ïà çà Ñ, òðàíñ äóê öèÿ ñèã íà ëà.
Î. Ì. ßêî âåí êî, Ñ. Â. Êðå òèí³í, Â. Ñ. Êðà âåöü
Ìî ëå êó ëÿðí³ îñíî âè ðåàë³çàö³¿ ñèã íàëü íî ãî øëÿ õó ôîñ ôà òè -
äèë³íî çè òîë-ñïå öèô³÷íî¿ ôîñ ôîë³ïàçè Ñ ó êë³òè íàõ ðîñ ëèí
Ðå çþ ìå
Ñèã íà ëè äîâê³ëëÿ ìî æóòü ñïðèé ìà òè ñÿ òà ïî ñè ëþ âà òè ñÿ â
êë³òè íàõ çà âäÿ êè ñèã íàëü íèì êàñ êà äàì. Ó ðîñ ëèí ôîñ ôàòè -
äèë³íî çè òîë-ñïå öèô³÷íà ôîñ ôîë³ïàçà Ñ (ÔËÑ) âè êî íóº âàæ ëè -
âó ðîëü ó êë³òèíí³é â³äïîâ³ä³ íà çîâí³øí³ ñòè ìó ëè. Ñó áñòðàò
òà ïðî äóê òè öüî ãî ôåð ìåí òó ðå ãó ëþ þòü ÷èñ ëåíí³ ïðî öå ñè â
êë³òè íàõ ðîñ ëèí. Â îãëÿä³ çî ñå ðåä æå íî óâà ãó íà ìî ëå êó ëÿð íèõ
îñíî âàõ ðåàë³çàö³¿ ñèã íàëü íî ãî øëÿ õó ôîñ ôàòè äèë³íî çè òîë-
ñïå öèô³÷íî¿ ÔËÑ. Àíàë³ç äà íèõ ìîæå äî ïîâ íè òè óÿâ ëåí íÿ ïðî
ìå õàí³çìè, ùî ëå æàòü â îñíîâ³ çäàò íîñò³ ðîñ ëèí ðå à ãó âà òè íà
ð³çíî ìàí³òí³ àá³îò è÷í³ òà á³îò è÷í³ ñòðå ñè.
Êëþ ÷îâ³ ñëî âà: ôîñ ôàòè äèë³íî çè òîë-ñïå öèô³÷íà ôîñ -
ôîë³ïàçà Ñ, òðàíñ äóêö³ÿ ñèã íà ëó.
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UDC 581.19
Received 20.09.08
452
IAKOVENKO O. M., KRETYNIN S. V., KRAVETS V. S.
|
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| institution | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| issn | 0233-7657 |
| language | Russian |
| last_indexed | 2025-12-07T17:36:55Z |
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| publisher | Інститут молекулярної біології і генетики НАН України |
| record_format | dspace |
| spelling | Яковенко, О.М. Кретинін, С.В. Кравец, В.С. 2019-06-21T05:35:00Z 2019-06-21T05:35:00Z 2008 Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин / О.М. Яковенко, С.В. Кретинін, В.С. Кравець // Біополімери і клітина. — 2008. — Т. 24, № 6. — С. 441-452. — Бібліогр.: 86 назв. — укр., англ. 0233-7657 DOI: http://dx.doi.org/10.7124/bc.0007BC https://nasplib.isofts.kiev.ua/handle/123456789/157882 581.19 Сигналы из окружающей среды могут восприниматься и усиливаться в клетках с помощью сигнальных каскадов. У растений фосфатидилинозитол-специфическая фосфолипаза С (ФЛС) выполняет важную роль в клеточном ответе на внешние стимулы. Субстрат и продукты ФЛС регулируют множество процессов в клетках растений. В настоящем обзоре мы сосредоточили внимание на молекулярных основах реализации сигнального пути фосфатидилинозитол-специфической ФЛС. Анализ данных поможет расширить представление о механизмах, лежащих в основе способности растений реагировать на разнообразные абиотические и биотические стрессы. Сигнали довкілля можуть сприйматися та посилюватися в клітинах завдяки сигнальним каскадам. У рослин фосфатидилінозитол-специфічна фосфоліпаза С (ФЛС) виконує важливу роль у клітинній відповіді на зовнішні стимули. Субстрат та продукти цього ферменту регулюють численні процеси в клітинах рослин. В огляді зосереджено увагу на молекулярних основах реалізації сигнального шляху фосфатидилінозитол- специфічної ФЛС. Аналіз даних може доповнити уявлення про механізми, що лежать в основі здатності рослин реагувати на різноманітні абіотичні та біотичні стреси. In plants external stimulus can be perceived and amplified in the cells by functional signaling cascades. Phosphoinositide-specific phospholipase C is an enzyme shown to initiate and provide key events in the cellular responses to extracellular signals. Both substrate and products of phospholipase C are involved in the regulation of numerous processes in plant cells. In this review, we focused on molecular basis of the phosphoinositide-specific phospholipase C signaling pathways. The data analyzed will help to elucidate the mechanisms responsible for plant’s ability to respond to a variety of biotic and abiotic stress signals. ru Інститут молекулярної біології і генетики НАН України Біополімери і клітина Огляди Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин Молекулярные основы реализации сигнального пути фосфатидилинозитол-специфической фосфолипазы С в клетках растений Molecular basis of phosphoinositide-specific phospholipase C signaling pathways in plant cells Article published earlier |
| spellingShingle | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин Яковенко, О.М. Кретинін, С.В. Кравец, В.С. Огляди |
| title | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин |
| title_alt | Молекулярные основы реализации сигнального пути фосфатидилинозитол-специфической фосфолипазы С в клетках растений Molecular basis of phosphoinositide-specific phospholipase C signaling pathways in plant cells |
| title_full | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин |
| title_fullStr | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин |
| title_full_unstemmed | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин |
| title_short | Молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази С у клітинах рослин |
| title_sort | молекулярні основи реалізації сигнального шляху фосфатидилінозитол-специфічної фосфоліпази с у клітинах рослин |
| topic | Огляди |
| topic_facet | Огляди |
| url | https://nasplib.isofts.kiev.ua/handle/123456789/157882 |
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