cofilin-1; cofilin, non-muscle isoform; 18 kD phosphoprotein; p18 (CFL1 CFL)
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Function
- cofilin has weak F-actin severing activity
- binds to actin monomers
- appears to 'nibble' monomer from F-actin leaving free barbed end
- action similar to destrin
- phospholipid binding may reduce affinity for G-actin[1]
- phosphorylation deactivates cofilin; dephosphorylation activates.
- phosphorylated by LIMK1
- dephosphorylated by SSH2, SSH3.
- binding of cofilin to actin displaces drebrin-bound to actin
Expression
- found in a variety of tissues
Pathology
- disulfide formation involving Cys39 & Cys147 result in an oligomer that induces abnormal actin-bundling activity & formation of Hirano bodies
More general terms
Additional terms
References
- ↑ Jump up to: 1.0 1.1 Pfannstiel J, Cyrklaff M, Habermann A, Stoeva S, Griffiths G, Shoeman R, Faulstich H. Human cofilin forms oligomers exhibiting actin bundling activity. J Biol Chem. 2001 Dec 28;276(52):49476-84. Epub 2001 Oct 25. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11679578
- ↑ UniProt http://www.uniprot.org/uniprot/P23528.html
- ↑ Wikipedia; Note: cofilin http://en.wikipedia.org/wiki/cofilin