CDPKs – a kinase for every Ca2+ signal?

Harmon, Alice C.; Gribskov, Michael; Harper, Jeffrey F.

doi:10.1016/s1360-1385(00)01577-6

Cited by 464 publications

(367 citation statements)

References 43 publications

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“…This result is supporting the model of CPKs activation that the binding of Ca 2+ can trigger conformational change of the kinase to release an auto-inhibitor from the active site [25]. In the absence of the calcium-binding Yun WANG et al domain, access to the active site is permanently blocked by the pseudosubstrate auto-inhibitor rendering the enzyme inactive [6].…”

Section: Analysis Of the Kinase Activity Of Ntcpk5 Proteinsupporting

confidence: 81%

“…1). NtCPK5 belongs to CPKs superfamily [5,6], comprising an N-terminal variable region, a kinase domain, a junction domain, and a Cterminal calmodulin-like domain with four EF-hand motifs implicated in Ca 2+ binding. The kinase domain (266 amino acids) of NtCPK5 contains all of the 11 conserved subdomains of Ser/Thr protein kinases including a putative ATP-binding site in the N-terminal region and a Ser/ Thr protein kinase active site in the center of the kinase domain.…”

Section: Molecular Cloning Of Ntcpk5mentioning

confidence: 99%

“…CPK-related protein kinases (CRKs) have both kinase domain and junction domain closely related to those of CDPKs, while their C-terminal domains have degenerated EF-hands [6]. Biochemical analyses showed that the activation of CRKs does not require calcium [13,24,27].…”

Section: Subcellular Localization Of Ntcpk5mentioning

confidence: 99%

“…Junction domain can serve as a pseudosubstrate and block the catalytic pocket of kinase domain in the absence of calcium. Upon the calcium binding to EF-hands, junction domain (the autoinhibitory region) is released from the kinase domain to activate CPKs [6].…”

Section: Introductionmentioning

confidence: 99%

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Cellular localization and biochemical characterization of a novel calcium-dependent protein kinase from tobacco

Wang

Zhang

et al. 2005

Cell Res

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By screening tobacco cDNA library with MCK1 as a probe, we isolated a cDNA clone NtCPK5 (accession number AY971376), which encodes a typical calcium-dependent protein kinase. Sequence analyses indicated that NtCPK5 is related to both CPKs and CRKs superfamilies and has all of the three conserved domains of CPKs. The biochemical activity of NtCPK5 was calcium-dependent. NtCPK5 had V max and K m of 526 nmol/min/mg and 210 µg/ml respectively with calf thymus histone (fraction III, abbreviated to histone IIIs) as substrate. For substrate syntide-2, NtCPK5 showed a higher V max of 2008 nmol/min/mg and a lower K m of 30 µM. The K 0.5 of calcium activation was 0.04 µM or 0.06 µM for histone IIIs or syntide-2 respectively. The putative myristoylation and palmitoylation consensus sequence of NtCPK5 suggests that it could be a membrane-anchoring protein. Indeed, our transient expression experiments with wild type and mutant forms of NtCPK5/GFP fusion proteins showed that NtCPK5 was localized to the plasma membrane of onion epidermal cells and that the localization required the N-terminal acylation sites of NtCPK5/GFP. Taking together, our data have demonstrated the biochemical characteristics of a novel protein NtCPK5 and its subcellular localization as a membrane-anchoring protein.

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Section: Analysis Of the Kinase Activity Of Ntcpk5 Proteinsupporting

confidence: 81%

Section: Molecular Cloning Of Ntcpk5mentioning

confidence: 99%

Section: Subcellular Localization Of Ntcpk5mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cellular localization and biochemical characterization of a novel calcium-dependent protein kinase from tobacco

Wang

Zhang

et al. 2005

Cell Res

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“…The homology to the liverwort Marchantia or the moss Tortula CDPKs was lower (59-64 %). The 70 kDa moss CCaMK belongs to another very important class of the calcium-regulated PKs that have a kinase domain followed by a CaM-binding domain homologous to neural visinin-like molecules (Harmon et al, 2000). The purified moss 70 kDa PK prefers lysine-rich histone as substrate and is fully active in the presence of 50 mM free calcium (D'Souza and Johri, 2003).…”

Section: Role Of Calcium In Bryophytesmentioning

confidence: 99%

Hormonal regulation in green plant lineage families

Johri

2008

Physiol Mol Biol Plants

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The patterns of phytohormones distribution, their native function and possible origin of hormonal regulation across the green plant lineages (chlorophytes, charophytes, bryophytes and tracheophytes) are discussed. The five classical phytohormonesauxins, cytokinins, gibberellins (GA), abscisic acid (ABA) and ethylene occur ubiquitously in green plants. They are produced as secondary metabolites by microorganisms. Some of the bacterial species use phytohormones to interact with the plant as a part of their colonization strategy. Phytohormone biosynthetic pathways in plants seem to be of microbial origin and furthermore, the origin of high affinity perception mechanism could have preceded the recruitment of a metabolite as a hormone. The bryophytes represent the earliest land plants which respond to the phytohormones with the exception of gibberellins. The regulation by auxin and ABA may have evolved before the separation of green algal lineage. Auxin enhances rhizoid and caulonemal differentiation while cytokinins enhance shoot bud formation in mosses. Ethylene retards cell division but seems to promote cell elongation. The presence of responses specific to cytokinins and ethylene strongly suggest the origin of their regulation in bryophytes. The hormonal role of GAs could have evolved in some of the ferns where antheridiogens (compounds related to GAs) and GAs themselves regulate the formation of antheridia.During migration of life forms to land, the tolerance to desiccation may have evolved and is now observed in some of the microorganisms, animals and plants. Besides plants, sequences coding for late embryogenesis abundant-like proteins occur in the genomes of other anhydrobiotic species of microorganisms and nematodes. ABA acts as a stress signal and increases rapidly upon desiccation or in response to some of the abiotic stresses in green plants. As the salt stress also increases ABA release in the culture medium of cyanobacterium Trichormus variabilis, the recruitment of ABA in the regulation of stress responses could have been derived from prokaryotes and present at the level of common ancestor of green plants. The overall hormonal action mechanisms in mosses are remarkably similar to that of the higher plants. As plants are thought to be monophyletic in origin, the existence of remarkably similar hormonal mechanisms in the mosses and higher plants, suggests that some of the basic elements of regulation cascade could have also evolved at the level of common ancestor of plants. The networking of various steps in a cascade or the crosstalk between different cascades is variable and reflects the dynamic interaction between a species and its specific environment.

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The calcium‐dependent protein kinase (CDPK) and CDPK‐related kinase gene families in Hevea brasiliensis—comparison with five other plant species in structure, evolution, and expression

et al. 2016

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Calcium‐dependent protein kinases (CDPKs or CPKs) play important roles in various physiological processes of plants, including growth and development, stress responses and hormone signaling. Although the CDPK gene family has been characterized in several model plants, little is known about this gene family in Hevea brasiliensis (the Para rubber tree). Here, we characterize the entire H. brasiliensis CDPK and CDPK‐related kinase (CRK) gene families comprising 30 CDPK genes (HbCPK1 to 30) and nine CRK genes (HbCRK1 to 9). Structure and phylogeny analyses of these CDPK and CRK genes demonstrate evolutionary conservation in these gene families across H. brasiliensis and other plant species. The expression of HbCPK and HbCRK genes was investigated via Solexa sequencing in a range of experimental conditions (different tissues, phases of leaf development, ethylene treatment, and various abiotic stresses). The results suggest that HbCPK and HbCRK genes are important components in growth, development, and stress responses of H. brasiliensis. Parallel studies on the CDPK and CRK gene families were also extended to five other plant species (Arabidopsis thaliana, Oryza sativa, Populus trichocarpa, Manihot esculenta, and Ricinus communis). The CDPK and CRK genes from different plant species that exhibit similar expression patterns tend to cluster together, suggesting a coevolution of gene structure and expression behavior in higher plants. The results serve as a foundation to further functional studies of these gene families in H. brasiliensis as well as in the whole plant kingdom.

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CDPKs – a kinase for every Ca2+ signal?

Cited by 464 publications

References 43 publications

Cellular localization and biochemical characterization of a novel calcium-dependent protein kinase from tobacco

Cellular localization and biochemical characterization of a novel calcium-dependent protein kinase from tobacco

Hormonal regulation in green plant lineage families

The calcium‐dependent protein kinase (CDPK) and CDPK‐related kinase gene families in Hevea brasiliensis—comparison with five other plant species in structure, evolution, and expression

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