Cofilin 1 Explained

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

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

Further reading

Notes and References

  1. Web site: Entrez Gene: CFL1 cofilin 1 (non-muscle).
  2. Chai X, Förster E, Zhao S, Bock HH, Frotscher M . Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3 . . 29 . 1 . 288–99 . January 2009 . 19129405 . 6664910 . 10.1523/JNEUROSCI.2934-08.2009 .
  3. Frotscher M, Chai X, Bock HH, Haas CA, Förster E, Zhao S . Role of Reelin in the development and maintenance of cortical lamination . . 116 . 11 . 1451–5 . April 2009 . 19396394 . 10.1007/s00702-009-0228-7 . 1310387 .
  4. Saito Y, Doi K, Yamagishi N, Ishihara K, Hatayama T . Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems . Biochem. Biophys. Res. Commun. . 314 . 2 . 396–402 . Feb 2004 . 14733918 . 10.1016/j.bbrc.2003.12.108 .
  5. Foletta VC, Lim MA, Soosairajah J, Kelly AP, Stanley EG, Shannon M, He W, Das S, Massague J, Bernard O, Soosairaiah J . Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1 . J. Cell Biol. . 162 . 6 . 1089–98 . Sep 2003 . 12963706 . 2172847 . 10.1083/jcb.200212060 .
  6. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S . Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase . . 285 . 5429 . 895–8 . Aug 1999 . 10436159 . 10.1126/science.285.5429.895 .