Cofilin 1

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
CFL1
Protein CFL1 PDB 1q8g.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCFL1, CFL, HEL-S-15, cofilin, cofilin 1
External IDsOMIM: 601442 MGI: 101757 HomoloGene: 99735 GeneCards: CFL1
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for CFL1
Genomic location for CFL1
Band11q13.1Start65,823,022 bp[1]
End65,862,026 bp[1]
RNA expression pattern
PBB GE CFL1 200021 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005507

NM_007687

RefSeq (protein)

NP_005498

NP_031713

Location (UCSC)Chr 11: 65.82 – 65.86 MbChr 19: 5.49 – 5.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5]

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.[6][7]

Interactions[edit]

Cofilin 1 has been shown to interact with HSPH1[8] and LIMK1.[9][10]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172757 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000056201 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ "Entrez Gene: CFL1 cofilin 1 (non-muscle)".
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.

Further reading[edit]