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. 2001 Jun 15;499(1-2):97-100.
doi: 10.1016/s0014-5793(01)02528-5.

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

E G Allwood  1 , A P Smertenko, P J Hussey
Affiliations
Free article

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

E G Allwood et al. FEBS Lett. .
Free article

Abstract

The 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-aminohexyl)-[(3)H]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 ADF is phosphorylated by CDPK(s), a class of protein kinases unique to plants and protozoa.

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