Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase

被引：78

作者：

Allwood, EG ^{[1
]}

Smertenko, AP ^{[1
]}

Hussey, PJ ^{[1
]}

机构：

[1] Univ Durham, Dept Biol Sci, Durham DH1 3LE, England

来源：

FEBS LETTERS | 2001年 / 499卷 / 1-2期

关键词：

actin-depolymerizing factor; calmodulin-like domain protein kinase; cofilin; phosphorylation; higher plant; cytoskeleton;

D O I：

10.1016/S0014-5793(01)02528-5

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：

actin-depolymerising factor (ADF)/cofilin group of proteins are stimulus-responsive actin-severing proteins, members of which are regulated by reversible phosphorylation. The phosphorylation site on the maize ADF, ZmADF3, is Ser-6 but the kinase responsible is unknown [Smertenko et al,, Plant J. 14 (1998) 187-193]. We have partially purified the ADF kinase(s) and found it to be calcium-regulated and inhibited by N-(6-aminohesyl)-[H-3]5-chloro-1-naphthalenesulphonamide. Immunoblotting reveals that calmodulin-like domain protein kinase(s) (CDPK) are enriched in the purified preparation and addition of anti-CDPK to in vitro phosphorylation assays results in the inhibition of ADF phosphorylation, These data strongly suggest that plant ADP is phosphorylation by CDPK(s), a class of protein kinases unique to plants and protozoa. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：97 / 100

页数：4

共 37 条

[1] REACTIVATION OF PHOSPHORYLATED ACTIN DEPOLYMERIZING FACTOR AND IDENTIFICATION OF THE REGULATORY SITE [J].