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
Identifiers
Symbols CFL1 ; CFL; HEL-S-15
External IDs OMIM601442 MGI101757 HomoloGene99735 ChEMBL: 1075129 GeneCards: CFL1 Gene
RNA expression pattern
PBB GE CFL1 200021 at tn.png
More reference expression data
Orthologs
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:
65.59 – 65.63 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]

Interactions[edit]

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

References[edit]

  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, Youhei; Doi Kazuya; Yamagishi Nobuyuki; Ishihara Keiichi; Hatayama Takumi (Feb 2004). "Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems". Biochem. Biophys. Res. Commun. (United States) 314 (2): 396–402. doi:10.1016/j.bbrc.2003.12.108. ISSN 0006-291X. PMID 14733918. 
  5. ^ Foletta, Victoria C; Lim Mei Ann, Soosairajah Juliana, Kelly April P, Stanley Edouard G, Shannon Mark, He Wei, Das Supratik, Massague Joan, Bernard Ora, Soosairaiah Juliana (Sep 2003). "Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1". J. Cell Biol. (United States) 162 (6): 1089–98. doi:10.1083/jcb.200212060. ISSN 0021-9525. 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 (UNITED STATES) 285 (5429): 895–8. doi:10.1126/science.285.5429.895. ISSN 0036-8075. PMID 10436159. 

Further reading[edit]