Autophosphorylation-based Calcium (Ca²⁺) Sensitivity Priming and Ca²⁺/Calmodulin Inhibition of Arabidopsis thaliana Ca²⁺-dependent Protein Kinase 28 (CPK28).

ABSTRACT: Plant calcium (Ca²⁺)-dependent protein kinases (CPKs) represent the primary Ca²⁺-dependent protein kinase activities in plant systems. CPKs are composed of a dual specificity (Ser/Thr and Tyr) kinase domain tethered to a calmodulin-like domain (CLD) via an autoinhibitory junction (J). Although regulation of CPKs by Ca²⁺ has been extensively studied, the contribution of autophosphorylation in controlling CPK activity is less well understood. Furthermore, whether calmodulin (CaM) contributes to CPK regulation, as is the case for Ca²⁺/CaM-dependent protein kinases outside the plant lineage, remains an open question. We therefore screened a subset of plant CPKs for CaM binding and found that CPK28 is a high affinity Ca²⁺/CaM-binding protei

SUBMITTER: Bender KW 

PROVIDER: S-EPMC5354511 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature