Abstract
BackgroundThe calcineurin B-like protein (CBL)-interacting protein kinase (CIPK) signaling pathway responds to various abiotic stresses in plants.ResultsWheat CIPK23, isolated from wheat drought transcriptome data set, was induced by multiple abiotic stresses, including drought, salt, and abscisic acid (ABA). Compared with wild-type plants, TaCIPK23-overexpression wheat and Arabidopsis showed an higher survival rate under drought conditions with enhanced germination rate, developed root system, increased accumulation of osmolytes, and reduced water loss rate. Over-expression of TaCIPK23 rendered transgenic plants ABA sensitivity, as evidenced by delayed seed germination and the induction of stomatal closure. Consistent with the ABA-sensitive phenotype, the expression level of drought- and ABA-responsive genes were increased under drought conditions in the transgenic plants. In addition, using yeast two-hybrid system, pull-down and bimolecular fluorescence complementation (BiFc) assays, TaCIPK23 was found to interact with TaCBL1 on the plasma membrane.ConclusionsThese results suggest that TaCIPK23 plays important roles in ABA and drought stress responses, and mediates crosstalk between the ABA signaling pathway and drought stress responses in wheat.
Highlights
The calcineurin B-like protein (CBL)-interacting protein kinase (CIPK) signaling pathway responds to various abiotic stresses in plants
TaCIPK23 enhanced the expression of a group of drought- and abscisic acid (ABA)-responsive genes under drought stress conditions. These results reveal a positive role for TaCIPK23 in conferring drought tolerance and regulating ABA signaling in plants
TaCIPK23 was included in subgroup I (Additional file 1: Figure S1)
Summary
The calcineurin B-like protein (CBL)-interacting protein kinase (CIPK) signaling pathway responds to various abiotic stresses in plants. Calcium (Ca2+) serves as a ubiquitous secondary messenger that is involved in multiple physiological and developmental processes in plants [3, 4]. Ca2+ sensor proteins, including Ca2+-dependent protein kinases (CDPKs), calmodulins (CAMs), and calcineurin B-like proteins (CBLs), decode these specific signatures and interact with targeted proteins to relay signals [6,7,8]. CBLs harbor four elongation factor (EF) hand motifs as the structural basis for Ca2+ binding These EF hands target a group of CDPKs designated as the CBL-interacting protein kinases (CIPKs) [9].
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