Cofilin-2

CFL2
Identifiers
Aliases	CFL2 , NEM7, cofilin 2
External IDs	OMIM: 601443 MGI: 101763 HomoloGene: 129115 GeneCards: CFL2
Gene location (Human)
Chr.	Chromosome 14 (human)
End	34,714,823 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	54,909,662 bp
RNA expression pattern
	Top expressed in
	deltoid muscle; ; tibialis anterior muscle; ; quadriceps femoris muscle; ; vastus lateralis muscle; ; biceps brachii; ; right ventricle; ; gastrocnemius muscle; ; corpus callosum; ; body of tongue; ; saphenous vein;
	Top expressed in
	intercostal muscle; ; atrioventricular valve; ; temporal muscle; ; sternocleidomastoid muscle; ; vastus lateralis muscle; ; triceps brachii muscle; ; ankle; ; atrium; ; digastric muscle; ; soleus muscle;
	More reference expression data
	n/a
Gene ontology
Molecular function	actin binding ; protein binding ; actin filament binding ;
Cellular component	nuclear matrix ; cytoplasm ; extracellular exosome ; intracellular anatomical structure ; cytoskeleton ; I band ; nucleus ; actin cytoskeleton ; Z disc ; extracellular space ;
Biological process	sarcomere organization ; muscle cell cellular homeostasis ; positive regulation of actin filament depolymerization ; actin filament organization ; actin filament depolymerization ; skeletal muscle tissue development ; actin filament fragmentation ;
	Sources:Amigo / QuickGO
Orthologs
	1073
	12632
	ENSG00000165410
	ENSMUSG00000062929
	Q9Y281 ; Q549N0
	P45591
	NM_001243645 ; NM_021914 ; NM_138638
	NM_007688
	NP_001230574 ; NP_068733 ; NP_619579 ; NP_068733.1 ; NP_619579.1 Contents Function ; Clinical significance ; References ; External links ; Further reading ;
	NP_031714
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 29, 2023

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

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.^[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

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]

Related Research Articles

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in many animal and fungal cells. In animals, it is an important component of the muscular system which works in conjunction with troponin to regulate muscle contraction. It is present in smooth and striated muscle tissues, which can be found in various organs and body systems, including the heart, blood vessels, respiratory system, and digestive system. In fungi, tropomyosin is found in cell walls and helps maintain the structural integrity of cells.

<span class="mw-page-title-main">Nebulin</span> Protein-coding gene in the species Homo sapiens

Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle. Nebulin in humans is coded for by the gene NEB. It is a very large protein and binds as many as 200 actin monomers. Because its length is proportional to thin filament length, it is believed that nebulin acts as a thin filament "ruler" and regulates thin filament length during sarcomere assembly and acts as the coats the actin filament. Other functions of nebulin, such as a role in cell signaling, remain uncertain.

ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation.

Cofilin 1 , also known as CFL1, is a human gene, part of the ADF/cofilin family.

<span class="mw-page-title-main">Destrin</span> Protein found in humans

Destrin or DSTN is a protein which in humans is encoded by the DSTN gene. Destrin is a component protein in microfilaments.

LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

F-actin-capping protein subunit alpha-1 is a protein that in humans is encoded by the CAPZA1 gene.

LIM domain and actin-binding protein 1 is a protein that in humans is encoded by the LIMA1 gene.

For the SSH-1 protocol, see Secure Shell#Version 1

Actin filament-associated protein 1 is a protein that in humans is encoded by the AFAP1 gene.

Protein phosphatase Slingshot homolog 2 is an enzyme that in humans is encoded by the SSH2 gene.

Protein phosphatase Slingshot homolog 3 is an enzyme that in humans is encoded by the SSH3 gene.

Leiomodin-3 is a protein that in humans is encoded by the LMOD3 gene. Leiomodin-3 is especially present at the pointed end of muscle thin filaments.

Twinfilin-1 is a protein that in humans is encoded by the TWF1 gene. This gene encodes twinfilin, an actin monomer-binding protein conserved from yeast to mammals. Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures may be regulated by the small GTPase RAC1.

Tropomodulin 4 (muscle) also known as TMOD4 is a protein which in humans is encoded by the TMOD4 gene.

In molecular biology, ADF-H domain is an approximately 150 amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000165410 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062929 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Entrez Gene: CFL2 cofilin 2 (muscle)".
1 2 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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

GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy
Human CFL2 genome location and CFL2 gene details page in the UCSC Genome Browser .

Thirion C, Stucka R, Mendel B, et al. (2001). "Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle". Eur. J. Biochem. 268 (12): 3473–82. doi: 10.1046/j.1432-1327.2001.02247.x . PMID 11422377.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Jia L, Young MF, Powell J, et al. (2002). "Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis". Genomics. 79 (1): 7–17. doi:10.1006/geno.2001.6683. PMID 11827452.
Kudryashov DS, Galkin VE, Orlova A, et al. (2006). "Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface". J. Mol. Biol. 358 (3): 785–97. doi:10.1016/j.jmb.2006.02.029. PMID 16530787.
Nebl G, Meuer SC, Samstag Y (1996). "Dephosphorylation of serine 3 regulates nuclear translocation of cofilin". J. Biol. Chem. 271 (42): 26276–80. doi: 10.1074/jbc.271.42.26276 . PMID 8824278.
Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell. Proteomics. 4 (9): 1240–50. doi: 10.1074/mcp.M500089-MCP200 . PMID 15951569.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129 . PMID 16344560.
Hillier LD, Lennon G, Becker M, et al. (1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi: 10.1101/gr.6.9.807 . PMID 8889549.
Endo M, Ohashi K, Sasaki Y, et al. (2003). "Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin". J. Neurosci. 23 (7): 2527–37. doi: 10.1523/JNEUROSCI.23-07-02527.2003 . PMC 6742113 . PMID 12684437.
Coiras M, Camafeita E, Ureña T, et al. (2006). "Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression". Proteomics. 6 Suppl 1: S63–73. doi:10.1002/pmic.200500437. PMID 16526095. S2CID 42878271.
Yang N, Higuchi O, Ohashi K, et al. (1998). "Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization". Nature. 393 (6687): 809–12. Bibcode:1998Natur.393..809Y. doi:10.1038/31735. PMID 9655398. S2CID 4326365.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID 17081983.
Wu Y, Yoder A, Yu D, et al. (2008). "Cofilin activation in peripheral CD4 T cells of HIV-1 infected patients: a pilot study". Retrovirology. 5 (1): 95. doi:10.1186/1742-4690-5-95. PMC 2576353 . PMID 18928553.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Papalouka V, Arvanitis DA, Vafiadaki E, et al. (2009). "Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle". Mol. Cell. Biol. 29 (22): 6046–58. doi:10.1128/MCB.00654-09. PMC 2772566 . PMID 19752190.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000165410 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000062929 - Ensembl, 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.

[entrez-5] "Entrez Gene: CFL2 cofilin 2 (muscle)".

[pmid8800436-6] 1 2 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.

[pmid10461190-7] 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.

[pmid12049672-8] 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.

[pmid11809832-9] 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.

[pmid11901171-10] 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.

[pmid17160903-11] 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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