Calmodulin-binding protein kinases in plants

Zhang, L

doi:10.1016/s1360-1385(03)00013-x

Cited by 111 publications

(91 citation statements)

References 34 publications

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“…Nonetheless, specific roles of CRKs in the control of root gravitropism remained thus far hidden because the available inhibitors and agonists could target more than one classes of signaling factors. The CaM antagonist KM-93 might thus interfere with the activities of CCaMK Ca 2+ and calmodulin-activated kinases, which carry visinin-like C-terminal Ca 2+ binding motives (Zhang and Lu, 2003), in addition to inhibiting CRKs that harbor defective Ca 2+ binding EF-hand motives, and are thus active also in the absence of Ca 2+ (Harper et al, 2004). Unlike some other plant species, intriguingly, no genuine CCaMK kinase is encoded by the Arabidopsis genome .…”

Section: Discussionmentioning

confidence: 99%

Inactivation of Plasma Membrane–Localized CDPK-RELATED KINASE5 Decelerates PIN2 Exocytosis and Root Gravitropic Response inArabidopsis

et al. 2013

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CRK5 is a member of the Arabidopsis thaliana Ca 2+ /calmodulin-dependent kinase-related kinase family. Here, we show that inactivation of CRK5 inhibits primary root elongation and delays gravitropic bending of shoots and roots. Reduced activity of the auxin-induced DR5-green fluorescent protein reporter suggests that auxin is depleted from crk5 root tips. However, no tip collapse is observed and the transcription of genes for auxin biosynthesis, AUXIN TRANSPORTER/AUXIN TRANSPORTER-LIKE PROTEIN (AUX/LAX) auxin influx, and PIN-FORMED (PIN) efflux carriers is unaffected by the crk5 mutation. Whereas AUX1, PIN1, PIN3, PIN4, and PIN7 display normal localization, PIN2 is depleted from apical membranes of epidermal cells and shows basal to apical relocalization in the cortex of the crk5 root transition zone. This, together with an increase in the number of crk5 lateral root primordia, suggests facilitated auxin efflux through the cortex toward the elongation zone. CRK5 is a plasma membrane-associated kinase that forms U-shaped patterns facing outer lateral walls of epidermis and cortex cells. Brefeldin inhibition of exocytosis stimulates CRK5 internalization into brefeldin bodies. CRK5 phosphorylates the hydrophilic loop of PIN2 in vitro, and PIN2 shows accelerated accumulation in brefeldin bodies in the crk5 mutant. Delayed gravitropic response of the crk5 mutant thus likely reflects defective phosphorylation of PIN2 and deceleration of its brefeldin-sensitive membrane recycling.

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Section: Discussionmentioning

confidence: 99%

Inactivation of Plasma Membrane–Localized CDPK-RELATED KINASE5 Decelerates PIN2 Exocytosis and Root Gravitropic Response inArabidopsis

et al. 2013

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“…The importance of Ca 2ϩ /CaM-meidated protein phosphorylation has been recognized in animals (23,45). Until recently, the understanding of the function of plant CaM-regulated kinases has been hindered by limited molecular and genetic tools (25). Characterization of CRCK1 and its homologs as CaM-regulated RLCKs is an important initial step in understanding the role of Ca 2ϩ /CaM-mediated phosphorylation in plants.…”

Section: Crck1 Is a Cam-binding Cytosolic Protein Kinase In Planta-mentioning

confidence: 99%

“…In plants, Ca 2ϩ /CaM-dependent protein phosphorylation was observed 2 decades ago (24). However, only two CaM-regulated kinases, which show overall homology to mammalian CaM kinases, have been reported to date, although there are a few other reported CaM-binding protein kinases (25). Our laboratory has reported that a chimeric Ca 2ϩ /CaM-dependent protein kinase (CCaMK) exhibits Ca 2ϩ -dependent autophosphorylation and Ca 2ϩ /CaM-dependent substrate phosphorylation (26,27).…”

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confidence: 99%

Calcium/Calmodulin Up-regulates a Cytoplasmic Receptor-like Kinase in Plants

Yang

Chaudhuri

Yang

et al. 2004

Journal of Biological Chemistry

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Calcium/calmodulin-dependent kinases play an important role in protein phosphorylation in eukaryotes. However, not much is known about calcium/calmodulin-dependent protein phosphorylation and its role in signal transduction in plants. By using a protein-protein interaction-based approach, we have isolated a novel plantspecific calmodulin-binding receptor-like cytoplasmic kinase (CRCK1) from Arabidopsis thaliana, as well as its ortholog from Medicago sativa (alfalfa). CRCK1 does not show high homology to calcium/calmodulin-dependent protein kinases in animals. In contrast, it shows high homology in the kinase domain to serine/threonine receptor-like kinases in plants. However, it contains neither a transmembrane domain nor an extracellular domain. Calmodulin binds to CRCK1 in a calcium-dependent manner with an affinity of ϳ20.5 nM. The calmodulin-binding site in CRCK1 is located in amino acids 160 -183, which overlap subdomain II of the kinase domain. CRCK1 undergoes autophosphorylation in the presence of Mg 2؉ at the threonine residue(s). The K m and V max values of CRCK1 for ATP are 1 M and 33.6 pmol/mg/min, respectively. Calcium/calmodulin stimulates the kinase activity of CRCK1, which increases the V max of CRCK1 ϳ9-fold. The expression of CRCK1 is increased in response to stresses such as cold and salt and stress molecules such as abscisic acid and hydrogen peroxide. These results indicate the presence of a calcium/calmodulin-regulated receptor-like cytoplasmic kinase in plants. Furthermore, these results also suggest that calcium/calmodulin-regulated protein phosphorylation involving CRCK1 plays a role in stress signal transduction in plants.

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“…fenugreek(T foenum -graecum callus induction was reported by (Aasim et al, 2009)in Fenugreek (T.foenum-graecumL.) hypocotyl explants were most responsive to callus induction and proliferation (Zhang et al, 2003). Thus, first of all, for biotechnological research on fenugreek(T.foenum -graecum a reliable callus induction protocol using hypocotyl is essential.Research on the medicinal aspects of fenugreek biproducts has taken great importance in the past few years (Bahram., 2005).…”

Section: Introductđonmentioning

confidence: 92%

In vitro Callus induction of Fenugreek (Trigonellafoenum-graecum L.) Using Different Media with Different Auxins Concentrations

Mawahib¹,

Lamia²

2013

ABJNA

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A protocol of callus induction in fenugreek (Trigonellafoenum-graecumL.) from 8 -20 days old in vitro grown cotyledons node explants cultured on Murashige and Skoog (MS) and B5 ((Gamborget al., 1958) media supplemented with different types and concentrations of growth regulators were tested in order to obtain the best callus formation. Two auxin types, α-naphthalene acetic acid (NAA), and 2,4-dichloro-phenoxyacetic acid (2,4-D) at four concentrations(0.5, 0.1, 1.5, and 2.0 mgL-1) with (0,0) as control in the two media were used in this study .The objective of this study was to determine the effect of different concentration of two types of auxins 2,4-D (2,4Dichlorophenoxy acetic acid) and NAA (Naphthalene acetic acid), on callus induction using cotyledons and hypocotyls explants of T.foenum -graecum. 100 percentage of primary callus induction rate and 2.5 callusing index were achieved on MS medium containing 2mg/l ,2,4-D hormone hypocotyls explants .The maximum value of callusing index (2.8) was obtained from MS medium containing 1.5 mg/l ,2,4-D using hypocotyls and cotyledons explants. The maximum callus formation observed in the MS media containing 2.0mg/l NAA was 3.9±o.o8 in hypocotyls segment. The callus was compact in cotyledons and variable in hypocotyls segments and the colour is creamy.

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Calmodulin-binding protein kinases in plants

Cited by 111 publications

References 34 publications

Inactivation of Plasma Membrane–Localized CDPK-RELATED KINASE5 Decelerates PIN2 Exocytosis and Root Gravitropic Response inArabidopsis

Inactivation of Plasma Membrane–Localized CDPK-RELATED KINASE5 Decelerates PIN2 Exocytosis and Root Gravitropic Response inArabidopsis

Calcium/Calmodulin Up-regulates a Cytoplasmic Receptor-like Kinase in Plants

In vitro Callus induction of Fenugreek (Trigonellafoenum-graecum L.) Using Different Media with Different Auxins Concentrations

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