Cofilin-2

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Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the CFL2 gene.[5][6]

CFL2
Identifiers
AliasesCFL2, NEM7, cofilin 2
External IDsOMIM: 601443; MGI: 101763; HomoloGene: 129115; GeneCards: CFL2; OMA:CFL2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001243645
NM_021914
NM_138638

NM_007688

RefSeq (protein)

NP_001230574
NP_068733
NP_619579
NP_068733.1
NP_619579.1

NP_031714

Location (UCSC)Chr 14: 34.71 – 34.71 MbChr 12: 54.91 – 54.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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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.[6] 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.[7][8] The CFL2 gene encodes a skeletal muscle-specific isoform[9] localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins.[10]

Clinical significance

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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.[11]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165410Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062929Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: CFL2 cofilin 2 (muscle)".
  6. ^ 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. S2CID 19565638.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
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Further reading

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