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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Allwood EG,Smertenko AP,Hussey PJ

doi

10.1016/s0014-5793(01)02528-5

keywords:

subject

Has Abstract

pub_date

2001-06-15 00:00:00

pages

97-100

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02528-5

journal_volume

499

pub_type

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