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cofilin-1; cofilin, non-muscle isoform; 18 kD phosphoprotein; p18 (CFL1 CFL)
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
Related
actin
Hirano body
General
cofilin
Properties
SIZE: entity length = 166 aa
MW = 19 kD
COMPARTMENT: cytoplasm
cell nucleus
MOTIF: acetylation site
SITE: N-TERMINUS
EFFECTOR-BOUND: acetyl
Ser phosphorylation site {S3}
ADF-H {4-153}
MOTIF: Ser phosphorylation site {S8}
Thr phosphorylation site {T25}
nuclear translocation signal {30-34}
Ser phosphorylation site {S41}
Tyr phosphorylation site {Y68}
Tyr phosphorylation site {Y140}
Ser phosphorylation site {S156}
Database Correlations
OMIM 601442
UniProt P23528
Pfam PF00241
Entrez Gene 1072
Kegg hsa:1072
References
- 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: 11679578
- UniProt :accession P23528
- Wikipedia; Note: cofilin
http://en.wikipedia.org/wiki/cofilin