Molecular Plant Advance Access originally published online on February 8, 2008
Molecular Plant 2008 1(2):238-248; doi:10.1093/mp/ssn003
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Calcineurin-B-Like Protein CBL9 Interacts with Target Kinase CIPK3 in the Regulation of ABA Response in Seed Germination
a Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA
b Department of Plant Molecular Biology, University of Delhi South Campus, Benito Juarez Road, New Delhi-110021, India
c Present address: Department of Bio-Environmental Science, Sunchon National University, Suncheon, Jeonnam 540–742, Korea
d Present address: Department of Molecular Physiology and Biochemistry, National Institute of Agricultural Biotechnology, Suwon 441–707, Korea
1 To whom correspondence should be addressed. E-mail sluan{at}nature.berkeley.edu, fax (510) 642-4995, tel. (510) 642-6306
Calcium plays a vital role as a second messenger in many signaling pathways in plants. The calcineurin B-like proteins (CBLs) represent a family of plant calcium-binding proteins that function in calcium signaling by interacting with their interacting protein kinases (CIPKs). In our previous study, we have reported a role for one of the CBLs (CBL9) and one of the CIPKs (CIPK3) in ABA signaling. Here, we have shown that CBL9 and CIPK3 physically and functionally interact with each other in regulating the ABA responses. The CBL9 and CIPK3 proteins interacted with each other in the yeast two-hybrid system and when expressed in plant cells. The double mutant cbl9cipk3 showed the similar hypersensitive response to ABA as observed in single mutants (cbl9 or cipk3). The constitutively active form of CIPK3 genetically complemented the cbl9 mutant, indicating that CIPK3 function downstream of CBL9. Based on these findings, we conclude that CBL9 and CIPK3 act together in the same pathway for regulating ABA responses.
Key Words: ABA calcium CBL CIPK osmotic stress signal transduction