Cofilin 1

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Cofilin 1 (non-muscle)
Protein CFL1 PDB 1q8g.png
PDB rendering based on 1q8g.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CFL1 ; CFL; HEL-S-15; cofilin
External IDs OMIM601442 MGI101757 HomoloGene99735 ChEMBL: 1075129 GeneCards: CFL1 Gene
RNA expression pattern
PBB GE CFL1 200021 at tn.png
More reference expression data
Species Human Mouse
Entrez 1072 12631
Ensembl ENSG00000172757 ENSMUSG00000056201
UniProt P23528 P18760
RefSeq (mRNA) NM_005507 NM_007687
RefSeq (protein) NP_005498 NP_031713
Location (UCSC) Chr 11:
65.82 – 65.86 Mb
Chr 19:
5.49 – 5.49 Mb
PubMed search [1] [2]

Cofilin 1 (non-muscle; n-cofilin), also known as CFL1, is a human gene, part of the ADF/cofilin family.

Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.[1]

One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration.[2][3]


Cofilin 1 has been shown to interact with HSPH1[4] and LIMK1.[5][6]


  1. ^ "Entrez Gene: CFL1 cofilin 1 (non-muscle)". 
  2. ^ Chai X, Förster E, Zhao S, Bock HH, Frotscher M (January 2009). "Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3". J. Neurosci. 29 (1): 288–99. doi:10.1523/JNEUROSCI.2934-08.2009. PMID 19129405. 
  3. ^ Frotscher M, Chai X, Bock HH, Haas CA, Förster E, Zhao S (April 2009). "Role of Reelin in the development and maintenance of cortical lamination". J Neural Transm 116 (11): 1451–5. doi:10.1007/s00702-009-0228-7. PMID 19396394. 
  4. ^ Saito Y, Doi K, Yamagishi N, Ishihara K, Hatayama T (Feb 2004). "Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems". Biochem. Biophys. Res. Commun. 314 (2): 396–402. doi:10.1016/j.bbrc.2003.12.108. PMID 14733918. 
  5. ^ Foletta VC, Lim MA, Soosairajah J, Kelly AP, Stanley EG, Shannon M, He W, Das S, Massague J, Bernard O, Soosairaiah J (Sep 2003). "Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1". J. Cell Biol. 162 (6): 1089–98. doi:10.1083/jcb.200212060. PMC 2172847. PMID 12963706. 
  6. ^ Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S (Aug 1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159. 

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