CFL2 (gene)

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Cofilin 2 (muscle)
PDB 1tvj EBI.png
PDB rendering based on 1tvj.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CFL2 ; NEM7
External IDs OMIM601443 MGI101763 HomoloGene129115 GeneCards: CFL2 Gene
Species Human Mouse
Entrez 1073 12632
Ensembl ENSG00000165410 ENSMUSG00000062929
UniProt Q9Y281 P45591
RefSeq (mRNA) NM_001243645 NM_007688
RefSeq (protein) NP_001230574 NP_031714
Location (UCSC) Chr 14:
34.71 – 34.71 Mb
Chr 12:
54.86 – 54.86 Mb
PubMed search [1] [2]

Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.[1][2]


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.[2] 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.[3][4] The CFL2 gene encodes a skeletal muscle-specific isoform[5] localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins.[6]

Clinical significance[edit]

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.[7]


  1. ^ "Entrez Gene: CFL2 cofilin 2 (muscle)". 
  2. ^ a b Gillett GT, Fox MF, Rowe PS, Casimir CM, Povey S (May 1996). "Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14". Ann. Hum. Genet. 60 (Pt 3): 201–11. doi:10.1111/j.1469-1809.1996.tb00423.x. PMID 8800436. 
  3. ^ Bamburg JR, McGough A, Ono S (September 1999). "Putting a new twist on actin: ADF/cofilins modulate actin dynamics". Trends Cell Biol. 9 (9): 364–70. doi:10.1016/S0962-8924(99)01619-0. PMID 10461190. 
  4. ^ Maciver SK, Hussey PJ (2002). "The ADF/cofilin family: actin-remodeling proteins". Genome Biol. 3 (5): reviews3007. doi:10.1186/gb-2002-3-5-reviews3007. PMC 139363. PMID 12049672. 
  5. ^ Vartiainen MK, Mustonen T, Mattila PK; et al. (January 2002). "The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics". Mol. Biol. Cell 13 (1): 183–94. doi:10.1091/mbc.01-07-0331. PMC 65081. PMID 11809832. 
  6. ^ Ono S, Ono K (March 2002). "Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics". J. Cell Biol. 156 (6): 1065–76. doi:10.1083/jcb.200110013. PMC 2173459. PMID 11901171. 
  7. ^ Agrawal PB, Greenleaf RS, Tomczak KK, Lehtokari VL, Wallgren-Pettersson C, Wallefeld W, Laing NG, Darras BT, Maciver SK, Dormitzer PR, Beggs AH (January 2007). "Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2". Am. J. Hum. Genet. 80 (1): 162–7. doi:10.1086/510402. PMC 1785312. PMID 17160903. 

External links[edit]

Further reading[edit]

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