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

EG Allwood, AP Smertenko, PJ Hussey*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

83 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)97-100
Number of pages4
JournalFEBS Letters
Volume499
Issue number1-2
Publication statusPublished - 15 Jun 2001

Keywords

  • BINDING
  • CALCIUM
  • PURIFICATION
  • F-ACTIN
  • COFILIN
  • actin-depolymerizing factor
  • NITRATE REDUCTASE
  • DYNAMICS
  • higher plant
  • cofilin
  • IN-VIVO
  • cytoskeleton
  • IDENTIFICATION
  • phosphorylation
  • calmodulin-like domain protein kinase
  • FILAMENT TURNOVER

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