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 language | English |
---|---|
Pages (from-to) | 97-100 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 499 |
Issue number | 1-2 |
Publication status | Published - 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