Cofilin

ADF/cofilin is a family of actin-binding proteins which disassembles actin filaments. Three highly conserved and highly (70%-82%) identical genes belonging to this family have been described in humans and mice:

Actin-binding proteins regulate assembly and disassembly of actin filaments.Cofilin, a member of the ADF/cofilin family is actually a protein with 70% sequence identity to ADF, making it part of the ADF/cofilin family of small ADP-binding proteins. The protein binds to actin monomers and filaments, G actin and F actin, respectively. Cofilin causes depolymerization at the minus end of filaments, thereby preventing their reassembly. The protein is known to sever actin filaments by creating more positive ends on filament fragments. Cofilin/ADF(destrin) is likely to sever F-actin without capping and prefers ADP-actin. These monomers can be recycled by profilin, activating monomers to go back into filament form again by an ADP-to-ATP exchange. ATP-actin is then available for assembly.

Cofilin 1

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.

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.

Interactions

Cofilin 1 has been shown to interact with HSPH1 and LIMK1.

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Further reading

CFL2 (gene)

Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.

Function

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. Cofilin-2 is a member of the AC group of proteins that also includes cofilin-1 (CFL1) and destrin (DSTN), all of which regulate actin-filament dynamics. The CFL2 gene encodes a skeletal muscle-specific isoform localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins.

Clinical significance

Mutations in the CFL2 gene are associated with nemaline myopathy. Deficiency of cofilin-2 may result in reduced depolymerization of actin filaments, causing their accumulation in nemaline bodies, minicores, and, possibly concentric laminated bodies.

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Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.