scholarly journals Biochemical Characterization of Calcineurin B-Like-Interacting Protein Kinase in Vicia Guard Cells

2010 ◽  
Vol 51 (3) ◽  
pp. 408-421 ◽  
Author(s):  
Misumi Tominaga ◽  
Akiko Harada ◽  
Toshinori Kinoshita ◽  
Ken-ichiro Shimazaki
Keyword(s):  
Protein Kinase ◽  
Biochemical Characterization ◽  
Guard Cells ◽  
Interacting Protein ◽  
Calcineurin B

scholarly journals Isolation and characterization of a cDNA coding cowpea (Vigna unguiculata (L.) Walp.) calcineurin B-like protein-interacting protein kinase, VuCIPK1

2008 ◽  
Vol 25 (5) ◽  
pp. 437-445 ◽  
Author(s):  
Masakazu Imamura ◽  
Takashi Yuasa ◽  
Tomoko Takahashi ◽  
Nagisa Nakamura ◽  
Nang Myin Phyu Sin Htwe ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Vigna Unguiculata ◽  
Interacting Protein ◽  
Isolation And Characterization ◽  
Calcineurin B

Arabidopsis calcineurin B-like proteins differentially regulate phosphorylation activity of CBL-interacting protein kinase 9

2018 ◽  
Vol 475 (16) ◽  
pp. 2621-2636 ◽  
Author(s):  
Akhilesh K. Yadav ◽  
Saroj K. Jha ◽  
Sibaji K. Sanyal ◽  
Sheng Luan ◽  
Girdhar K. Pandey
Keyword(s):  
Kinase Activity ◽  
Biochemical Characterization ◽  
Cytosolic Calcium ◽  
Interacting Protein ◽  
Calcineurin B ◽  
K Deficiency ◽  
Metal Cofactors ◽  
Two Hybrid

Calcium (Ca2+) is a versatile and ubiquitous second messenger in all eukaryotes including plants. In response to various stimuli, cytosolic calcium concentration ([Ca2+]cyt) is increased, leading to activation of Ca2+ sensors including Arabidopsis calcineurin B-like proteins (CBLs). CBLs interact with CBL-interacting protein kinases (CIPKs) to form CBL–CIPK complexes and transduce the signal downstream in the signalling pathway. Although there are many reports on the regulation of downstream targets by CBL–CIPK module, knowledge about the regulation of upstream components by individual CIPKs is inadequate. In the present study, we have carried out a detailed biochemical characterization of CIPK9, a known regulator of K+ deficiency in Arabidopsis, with its interacting CBLs. The present study suggests that CIPK9 specifically interacts with four CBLs, i.e. CBL1, CBL2, CBL3 and CBL9, in yeast two-hybrid assays. Out of these four CBLs, CBL2 and CBL3, specifically enhance the kinase activity of CIPK9, while the CBL1 and CBL9 decrease it as examined by in vitro kinase assays. In contrast, truncated CIPK9 (CIPK9ΔR), without the CBL-interacting regulatory C-terminal region, is not differentially activated by interacting CBLs. The protein phosphorylation assay revealed that CBL2 and CBL3 serve as preferred substrates of CIPK9. CBL2– and CBL3–CIPK9 complexes show altered requirement for metal cofactors when compared with CIPK9 alone. Moreover, the autophosphorylation of constitutively active CIPK9 (CIPK9T178D) and less active CIPK9 (CIPK9T178A) in the presence of CBL2 and CBL3 was further enhanced. Our study suggests that CIPK9 differentially phosphorylates interacting CBLs, and furthermore, the kinase activity of CIPK9 is also differentially regulated by specific interacting CBLs.

scholarly journals The CBL–CIPK Pathway in Plant Response to Stress Signals

2020 ◽  
Vol 21 (16) ◽  
pp. 5668
Author(s):  
Xiao Ma ◽  
Quan-Hui Li ◽  
Ya-Nan Yu ◽  
Yi-Ming Qiao ◽  
Saeed ul Haq ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Future Research ◽  
Complex Environments ◽  
Yield Improvement ◽  
Interacting Protein ◽  
Secondary Messenger ◽  
Calcineurin B ◽  
Response To Stress ◽  
Stress Signals

Plants need to cope with multitudes of stimuli throughout their lifecycles in their complex environments. Calcium acts as a ubiquitous secondary messenger in response to numerous stresses and developmental processes in plants. The major Ca2+ sensors, calcineurin B-like proteins (CBLs), interact with CBL-interacting protein kinases (CIPKs) to form a CBL–CIPK signaling network, which functions as a key component in the regulation of multiple stimuli or signals in plants. In this review, we describe the conserved structure of CBLs and CIPKs, characterize the features of classification and localization, draw conclusions about the currently known mechanisms, with a focus on novel findings in response to multiple stresses, and summarize the physiological functions of the CBL–CIPK network. Moreover, based on the gradually clarified mechanisms of the CBL–CIPK complex, we discuss the present limitations and potential prospects for future research. These aspects may provide a deeper understanding and functional characterization of the CBL–CIPK pathway and other signaling pathways under different stresses, which could promote crop yield improvement via biotechnological intervention.

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