Protein Kinases and Phosphatases and Their Role in Cellular Signaling in Plants

Sopory, Sudhir K.; Munshi, Meenakshi

doi:10.1080/07352689891304230

Cited by 73 publications

(29 citation statements)

References 341 publications

(560 reference statements)

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“…Drought, salt, cold, light, and hormones can influence the expression or activity of various CDPKs in plants (Sopory and Munshi, 1998). Increased CDPK activity and Ca 2+ -dependent protein phosphorylation were observed in rice seedlings exposed to cold (Li and Komatsu, 2000;Komatsu et al, 2001) and hormone treatment (Kawasaki et al, 1993;Karibe and Komatsu, 1997;Yang and Komatsu, 2000).…”

Section: Introductionmentioning

confidence: 98%

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OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath

et al. 2004

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Calcium-dependent protein kinases (CDPKs) play an important role in rice signal transduction, but the precise role of each individual CDPK is still largely unknown. Recently, a full-length cDNA encoding OsCDPK13 from rice seedling was isolated. To characterize the function of OsCDPK13, its responses to various stresses and hormones were analyzed in this study. OsCDPK13 accumulated in 2-week-old leaf sheath and callus, and became phosphorylated in response to cold and gibberellin (GA). OsCDPK13 gene expression and protein accumulation were up-regulated in response to GA3 treatment, but suppressed in response to abscisic acid and brassinolide. Antisense OsCDPK13 transgenic rice lines were shorter than the vector control lines, and the expression of OsCDPK13 was lower in dwarf mutants of rice than in wild type. Furthermore, OsCDPK13 gene expression and protein accumulation were enhanced in response to cold, but suppressed under salt and drought stresses. Sense OsCDPK13 transgenic rice lines had higher recovery rates after cold stress than vector control rice. The expression of OsCDPK13 was stronger in cold-tolerant rice varieties than in cold-sensitive ones. The results suggest that OsCDPK13 might be an important signaling component in the response of rice to GA and cold stress.

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Section: Introductionmentioning

confidence: 98%

“…Calcium acts through various intracellular mediators, including calmodulin (CaM) and Ca 2+ -regulated kinases (Sopory and Munshi, 1998). Plants contain a novel group of kinases, designated as Ca 2+ -dependent protein kinases (CDPKs; EC 2.7.1.37), which are found only in plants, green algae, and protozoa (Hrabak, 2003).…”

Section: Introductionmentioning

confidence: 99%

OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath

et al. 2004

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“…In relation to this, a possible tyrosine phosphorylation of oat phytochrome A in the dark and its apparent decrease following red light treatment has been demonstrated (Sommer et al 1996). The role of Ca 2+ /CaM signaling in phytochrome signal transduction is well established (Millar et al 1994;Neuhaus et al 1997;Schafer et al 1997;Sopory and Munshi 1998). Furthermore, The role of protein kinase C phosphorylation in the regulation of the signal transduction chain pertaining to Ca 2+ /CaM signaling in receptor functioning is well known too.…”

Section: Structural Features Of the Wheat Phyc Genementioning

confidence: 92%

“…Whether these putative protein kinase C phosphorylation sites have a role in regulation of phytochrome signaling will be interesting to examine. There are, however, indications that phytochrome-mediated light regulation of NR and PHYI gene expression may involve certain common steps in the signal transduction pathway such as the PI cycle and protein phosphorylation by a PKC-type enzyme (Raghuram and Sopory 1995;Sopory and Munshi 1998).…”

Section: Structural Features Of the Wheat Phyc Genementioning

confidence: 97%

Structural characterization, expression analysis and evolution of the red/far-red sensing photoreceptor gene, phytochrome C (PHYC), localized on the ‘B’ genome of hexaploid wheat (Triticum aestivum L.)

Kulshreshtha

Kumar

Balyan

et al. 2005

Planta

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Phytochromes are a family of red/far-red light perceiving photoreceptors. The monocot phytochrome family is represented by three members, PHYA, PHYB and PHYC. We have isolated and characterized the first PHY gene member (TaPHYC) from common wheat, Triticum aestivum var. CPAN1676. It codes for a species of the photoreceptor, phyC, which is known to be light-stable in all plants analyzed so far. A sequence of 7.2 kb has been determined, which includes 3.42 kb of coding region. This is the second full-length PHYC gene sequenced from a monocot (first was from rice). TaPHYC gene shares structural similarities with the rice PHYC containing four exons and three introns in the coding region. The 5' UTR is 1.0-kb-long and harbors an upstream open reading frame (URF) encoding 28 aa. Southern blot analysis of TaPHYC indicates that it represents single locus in the wheat genome, although the possibility of additional loci cannot be completely ruled out. Chromosomal localization using nullisomic-tetrasomic lines of Triticum aestivum var. Chinese Spring places TaPHYC on chromosome 4B. PHYC represents a constitutively expressed gene in all the organs tested and under light/dark conditions. However, PHYC was found to be developmentally regulated showing maximal expression in 3-day-old dark-grown seedlings, which declined thereafter. In silico analysis has also been done to compare TaPHYC gene with the partial sequences known from other wheat species and cultivars. The presence of a topoisomerase gene immediately downstream of the PHYC gene, both in rice and wheat genomes, presents yet another example of synteny in cereals and its possible significance has been discussed.

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“…Prokaryotic organsims use His-to-Asp phosphotransfer, whereas eukaryotic signal transduction cascades are predominantly mediated by the reversible phosphorylation of Ser, Thr and Tyr [26,27]. Examples of eukaryotic protein histidine kinases also exist, and His-to-Asp phospho-relays have been proposed [28].…”

Section: Discussionmentioning

confidence: 99%

Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues

Thelen

Miernyk

Randall

2000

Biochemical Journal

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Pyruvate dehydrogenase kinase (PDK) is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex (PDC). Although PDKs inactivate mitochondrial PDC by phosphorylating specific Ser residues, the primary amino acid sequence indicates that they are more closely related to prokaryotic His kinases than to eukaryotic Ser/Thr kinases. Unlike Ser/Thr kinases, His kinases use a conserved His residue for phosphotransfer to Asp residues. To understand these unique kinases better, a presumptive PDK from Arabidopsis thaliana was heterologously expressed and purified for this investigation. Purified, recombinant A. thaliana PDK could inactivate kinase-depleted maize mitochondrial PDC by phosphorylating Ser residues. Additionally, A. thaliana PDK was capable of autophosphorylating Ser residues near its N-terminus, although this reaction is not part of the phosphotransfer pathway. To elucidate the mechanism involved, we performed site-directed mutagenesis of the canonical His residue likely to be involved in phosphotransfer. When His-121 was mutated to Ala or Gln, Ser-autophosphorylation was decreased by 50% and transphosphorylation of PDC was decreased concomitantly. We postulate that either (1) His-121 is not the sole phosphotransfer His residue or (2) mutagenesis of His-121 exposes an additional otherwise cryptic phosphotransfer His residue. Thus His-121 is one residue involved in kinase function.

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Protein Kinases and Phosphatases and Their Role in Cellular Signaling in Plants

Cited by 73 publications

References 341 publications

OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath

OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath

Structural characterization, expression analysis and evolution of the red/far-red sensing photoreceptor gene, phytochrome C (PHYC), localized on the ‘B’ genome of hexaploid wheat (Triticum aestivum L.)

Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues

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