CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity

被引:28
|
作者
Oh, Man-Ho [1 ]
Wu, Xia [1 ]
Kim, Hyoung Seok [1 ]
Harper, Jeffrey F. [2 ]
Zielinski, Raymond E. [1 ]
Clouse, Steven D. [3 ]
Huber, Steven C. [1 ,4 ]
机构
[1] Univ Illinois, Dept Plant Biol, Urbana, IL 61801 USA
[2] Univ Nevada, Dept Biochem & Mol Biol, Reno, NV 89557 USA
[3] NC State Univ, Dept Hort Sci, Raleigh, NC 27695 USA
[4] ARS, USDA, Urbana, IL 61801 USA
基金
美国国家科学基金会;
关键词
Calcium-dependent protein kinase; Tyrosine autophosphorylation; Site-directed mutagenesis; Calcium signaling; Peptide kinase activity; REGULATORY PHOSPHORYLATION SITE; SYNTHETIC PEPTIDES; CALCIUM; IDENTIFICATION; LOCALIZATION; SUPERFAMILY; RESIDUES; GENE;
D O I
10.1016/j.febslet.2012.09.040
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Although calcium-dependent protein kinases (CDPKs or CPKs) are classified as serine/threonine protein kinases, autophosphorylation on tyrosine residues was observed for soybean CDPK beta and several Arabidopsis isoforms (AtCPK4 and AtCPK34). We identified Ser-8, Thr-17, Tyr-24 (in the kinase domain), Ser-304, and Ser-358 as autophosphorylation sites of His(6)-GmCDPK beta. Overall autophosphorylation increased kinase activity with synthetic peptides, but autophosphorylation of Tyr-24 appears to attenuate kinase activity based on studies with the Y24F directed mutant. While much remains to be done, it is clear that several CDPKs are dual-specificity kinases, which raises the possibility that phosphotyrosine signaling may play a role in Ca2+/CDPK-mediated processes.
引用
收藏
页码:4070 / 4075
页数:6
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