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1 CDPK activated novel vacuolar chloride (VCL) and malate
2 CDPK enzymatic activity previously has been detected in
3 CDPK exhibits a Ca(2+)-induced electrophoretic mobility
4 CDPK from guard cells phosphorylates the K+ channel KAT1
5 CDPK-activated VCL currents were also observed in red be
6 CDPK-silenced plants showed a reduced and delayed hypers
7 CDPKs and at least one SnRK have been implicated in deco
8 CDPKs and SnRKs are found on all five Arabidopsis chromo
9 CDPKs are encoded by large multigene families, and to as
10 CDPKs are present in plants and a specific subgroup of p
11 CDPKs commonly have an N-terminal kinase domain (KD) and
12 CDPKs contain an autoinhibitory junction (J) region whos
13 CDPKs have diverse regulatory functions, including invol
14 CDPKs provide the first example of a member of the calmo
15 ysis of the Arabidopsis genome identified 34 CDPKs, eight CRKs, two PPCKs, two PEPRKs, and 38 SnRKs.
21 To understand how the CaM-LD regulates a CDPK, a recombinant CDPK (isoform CPK-1 from Arabidopsis
25 introns supports the phylogenetic analysis; CDPK genes with similar intron/exon structure are groupe
26 ulin-like domain, suggest that the ancestral CDPK gene could have originated from the fusion of prote
27 activity of MAPKs and CDPK-like kinases, and CDPK and NADPH oxidases were involved in As-induced MAPK
28 pecies and calcium and activity of MAPKs and CDPK-like kinases were induced with increasing Cr(VI) co
29 markedly increased the activity of MAPKs and CDPK-like kinases, and CDPK and NADPH oxidases were invo
30 itial kinetics of calmodulin stimulation and CDPK inhibition, providing an example in plants for a po
33 In this Update, we analyze the Arabidopsis CDPK gene family and review the expression, regulation,
34 roaches, the characterization of Arabidopsis CDPKs provides a valuable opportunity to understand the
37 s: calcium-dependent protein kinase (CDPKs), CDPK-related kinases (CRKs), phosphoenolpyruvate carboxy
38 pport a monophyletic origin for plant CDPKs, CDPK-related kinases, and phosphoenolpyruvate carboxylas
39 on, the interconversion of the corresponding CDPK forms could be induced in vitro in both directions
44 ed for half-maximal activity (K0.5) for each CDPK with syntide-2 as substrate were 0.06, 0.4, and 1 m
46 nsition from the nonelicited to the elicited CDPK form was caused by a phosphorylation event and was
48 g cascade in planta via unregulated enhanced CDPK activity can lead to off-type effects likely due to
51 ivated only 5-fold, but the activity of His6-CDPK alpha (1-398), which retained nearly half of the CL
52 of the chimeric enzyme, its addition to His6-CDPK alpha (1-398) resulted in activity that was only 6%
53 cal inhibitors indicated that the identified CDPK is independent of or is located upstream from a sig
54 bout the subcellular locations of individual CDPKs or the mechanisms involved in targeting them to th
56 domain by a Ca(2+)-dependent protein kinase (CDPK isoform CPK1), inhibits both basal activity ( appro
59 ht-induced calcium-dependent protein kinase (CDPK) isolated from the common ice plant, Mesembryanthem
60 An isoform of Ca2+-dependent protein kinase (CDPK) phosphorylated multiple sites of LlEF-1alpha1 in a
61 The native Ca(2+)-dependent protein kinase (CDPK) responsible for in vivo inhibitory phosphorylation
62 by a maize calcium-dependent protein kinase (CDPK) significantly increased sucrose cleavage activity
63 ane-bound, calcium-dependent protein kinase (CDPK) that showed a shift in electrophoretic mobility fr
64 responsive calcium-dependent protein kinase (CDPK) was isolated from the common ice plant (Mesembryan
65 APK) and 1 calcium-dependent protein kinase (CDPK) were upregulated with short-term Cr(VI) treatment.
66 za sativa) calcium-dependent protein kinase (CDPK), CPK18, was identified as an upstream kinase of MA
68 n kinases: calcium-dependent protein kinase (CDPKs), CDPK-related kinases (CRKs), phosphoenolpyruvate
72 ly inhibit select calcium-dependent kinases (CDPKs), we instead demonstrate that these pathways are c
73 constitutive Ca2+-dependent protein kinases (CDPKs) activate ABA responses, the MED141-143IGH and G18
74 fferent from Ca2+-dependent protein kinases (CDPKs) and other serine/threonine kinases in plants.
77 that four calcium-dependent protein kinases (CDPKs) are Ca(2+)-sensor protein kinases critical for tr
88 those of the Ca2+-dependent protein kinases (CDPKs) from Plasmodium, Eimeria, and several plants, and
89 for calmodulin-like domain protein kinases (CDPKs) have been identified in plants and Alveolate prot
90 parasite calcium-dependent protein kinases (CDPKs) have been shown to reduce infection in several pa
95 family of calcium-dependent protein kinases (CDPKs) that have no direct homologues in the human host.
96 ing novel calcium-dependent protein kinases (CDPKs) that provides new insights into the roles of CDPK
97 lant-like" Ca(2+)-dependent protein kinases (CDPKs) transduces cytosolic Ca(2+) flux into enzymatic a
101 The observation of a peroxisome-located CDPK suggests a mechanism for calcium regulation of pero
105 he subcellular targeting potentials for nine CDPK isoforms from Arabidopsis, as determined by express
107 (45) (S45/A) completely blocked the observed CDPK inhibition of both basal and calmodulin-stimulated
111 D to the autoinhibitory (junction) domain of CDPK alpha in a manner analogous to the activation of ca
114 n, recombinant CLD and truncation mutants of CDPK alpha were expressed in bacteria and highly purifie
115 crystal structure of the J-CaM-LD region of CDPK from Arabidopsis thaliana (AtCPK1), determined to 2
118 ntiality of CDPK1 and CDPK7, the majority of CDPKs had no discernible phenotype for growth in vitro o
120 This work reveals the critical roles of CDPKs in modulating JA homeostasis and highlights the co
121 l with the consensus phosphorylation site of CDPKs, its coding sequence was cloned and stably transfo
122 show that this kinase and a number of other CDPKs of similar Mr showed complex changes in elicitor-t
123 PfCDPK7 is very different from that of other CDPKs; it has a pleckstrin homology domain adjacent to t
126 amecium genes differ from those in the plant CDPK genes in about 20 of 31 residues in the junction re
128 The introns shared between protist and plant CDPKs presumably originated before the divergence of pla
130 rons support a monophyletic origin for plant CDPKs, CDPK-related kinases, and phosphoenolpyruvate car
132 gether with previous studies on a plasmodium CDPK suggests a model whereby even at normally low cytos
135 ally, the calmodulin-like domains of protist CDPKs have intron positions in common with animal and fu
136 w the CaM-LD regulates a CDPK, a recombinant CDPK (isoform CPK-1 from Arabidopsis, accession no. L147
138 plants and ciliates, suggesting that related CDPKs may have a function in calcium-regulated secretion
140 ugh previous studies have shown that several CDPKs play a role in controlling invasion, egress, and c
141 dant roles in vivo, we characterized soybean CDPK isoforms alpha, beta, and gamma, which share 60-80%
147 tron placements supports the hypothesis that CDPKs, CRKs, PPCKs and PEPRKs have a common evolutionary
148 anscriptome profile comparison suggests that CDPKs are the convergence point of signalling triggered
152 To study the molecular evolution of the CDPK gene family, we performed a phylogenetic analysis o
156 hen elicitor is subsequently added while the CDPK cannot be activated by elicitor upon forskolin trea
161 ow Ca(2+) signaling activates egress through CDPKs, we performed a forward genetic screen to isolate
163 nition by CaM other features are specific to CDPKs, in particular the combination of the strong inter
164 revious studies on Plasmodium and Toxoplasma CDPKs suggest a role for the JD and CamLD in the regulat
167 nic Nicotiana attenuata plants, in which two CDPKs, NaCDPK4 and NaCDPK5, were simultaneously silenced
170 atter activity approached that of unmodified CDPK alpha and was half maximal at a CLD concentration o
171 se of catalytically impaired and unregulated CDPKs with the yeast two-hybrid system can accelerate th
172 sition was not inhibited by W-7, the in vivo CDPK activation probably is not the result of autophosph
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