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==Function== |
==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.<ref name="pmid8800436"/> Cofilin-2 is a member of the AC group of proteins that also includes cofilin-1 ([[CFL1]]) and destrin ([[Destrin|DSTN]]), all of which regulate actin-filament dynamics.<ref name="pmid10461190">{{cite journal | vauthors = Bamburg JR, McGough A, Ono S | title = Putting a new twist on actin: ADF/cofilins modulate actin dynamics | journal = Trends Cell Biol. | volume = 9 | issue = 9 | pages = 364–70 |date=September 1999 | pmid = 10461190 | doi = 10.1016/S0962-8924(99)01619-0}}</ref><ref name="pmid12049672">{{cite journal | vauthors = Maciver SK, Hussey PJ | title = The ADF/cofilin family: actin-remodeling proteins | journal = Genome Biol. | volume = 3 | issue = 5 | pages = reviews3007 | year = 2002 | pmid = 12049672 | pmc = 139363 | doi = 10.1186/gb-2002-3-5-reviews3007}}</ref> The CFL2 gene encodes a skeletal muscle-specific isoform<ref name="pmid11809832">{{cite journal | vauthors = Vartiainen MK, Mustonen T, Mattila PK | title = The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics | journal = Mol. Biol. Cell | volume = 13 | issue = 1 | pages = 183–94 |date=January 2002 | pmid = 11809832 | pmc = 65081 | doi = 10.1091/mbc.01-07-0331 |display-authors=etal}}</ref> localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins.<ref name="pmid11901171">{{cite journal | vauthors = Ono S, Ono K | title = Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics | journal = J. Cell Biol. | volume = 156 | issue = 6 | pages = 1065–76 |date=March 2002 | pmid = 11901171 | pmc = 2173459 | doi = 10.1083/jcb.200110013 }}</ref> |
[[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.<ref name="pmid8800436"/> Cofilin-2 is a member of the AC group of proteins that also includes cofilin-1 ([[CFL1]]) and destrin ([[Destrin|DSTN]]), all of which regulate actin-filament dynamics.<ref name="pmid10461190">{{cite journal | vauthors = Bamburg JR, McGough A, Ono S | title = Putting a new twist on actin: ADF/cofilins modulate actin dynamics | journal = Trends Cell Biol. | volume = 9 | issue = 9 | pages = 364–70 |date=September 1999 | pmid = 10461190 | doi = 10.1016/S0962-8924(99)01619-0}}</ref><ref name="pmid12049672">{{cite journal | vauthors = Maciver SK, Hussey PJ | title = The ADF/cofilin family: actin-remodeling proteins | journal = Genome Biol. | volume = 3 | issue = 5 | pages = reviews3007 | year = 2002 | pmid = 12049672 | pmc = 139363 | doi = 10.1186/gb-2002-3-5-reviews3007 | doi-access = free }}</ref> The CFL2 gene encodes a skeletal muscle-specific isoform<ref name="pmid11809832">{{cite journal | vauthors = Vartiainen MK, Mustonen T, Mattila PK | title = The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics | journal = Mol. Biol. Cell | volume = 13 | issue = 1 | pages = 183–94 |date=January 2002 | pmid = 11809832 | pmc = 65081 | doi = 10.1091/mbc.01-07-0331 |display-authors=etal}}</ref> localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins.<ref name="pmid11901171">{{cite journal | vauthors = Ono S, Ono K | title = Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics | journal = J. Cell Biol. | volume = 156 | issue = 6 | pages = 1065–76 |date=March 2002 | pmid = 11901171 | pmc = 2173459 | doi = 10.1083/jcb.200110013 }}</ref> |
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==Clinical significance== |
==Clinical significance== |
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*{{cite journal |vauthors=Hillier LD, Lennon G, Becker M |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1996 |pmid= 8889549 |doi=10.1101/gr.6.9.807 |display-authors=etal|doi-access=free }} |
*{{cite journal |vauthors=Hillier LD, Lennon G, Becker M |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1996 |pmid= 8889549 |doi=10.1101/gr.6.9.807 |display-authors=etal|doi-access=free }} |
||
*{{cite journal |vauthors=Endo M, Ohashi K, Sasaki Y |title=Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin. |journal=J. Neurosci. |volume=23 |issue= 7 |pages= 2527–37 |year= 2003 |pmid= 12684437 |doi= 10.1523/JNEUROSCI.23-07-02527.2003|pmc=6742113 |display-authors=etal|doi-access=free }} |
*{{cite journal |vauthors=Endo M, Ohashi K, Sasaki Y |title=Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin. |journal=J. Neurosci. |volume=23 |issue= 7 |pages= 2527–37 |year= 2003 |pmid= 12684437 |doi= 10.1523/JNEUROSCI.23-07-02527.2003|pmc=6742113 |display-authors=etal|doi-access=free }} |
||
*{{cite journal |vauthors=Coiras M, Camafeita E, Ureña T |title=Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression. |journal=Proteomics |volume=6 |
*{{cite journal |vauthors=Coiras M, Camafeita E, Ureña T |title=Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression. |journal=Proteomics |volume=6 |pages= S63–73 |year= 2006 |issue=Suppl 1 |pmid= 16526095 |doi= 10.1002/pmic.200500437 |s2cid=42878271 |display-authors=etal}} |
||
*{{cite journal |vauthors=Yang N, Higuchi O, Ohashi K |title=Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. |journal=Nature |volume=393 |issue= 6687 |pages= 809–12 |year= 1998 |pmid= 9655398 |doi= 10.1038/31735 |bibcode=1998Natur.393..809Y |s2cid=4326365 |display-authors=etal}} |
*{{cite journal |vauthors=Yang N, Higuchi O, Ohashi K |title=Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. |journal=Nature |volume=393 |issue= 6687 |pages= 809–12 |year= 1998 |pmid= 9655398 |doi= 10.1038/31735 |bibcode=1998Natur.393..809Y |s2cid=4326365 |display-authors=etal}} |
||
*{{cite journal |vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal|doi-access=free }} |
*{{cite journal |vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal|doi-access=free }} |
||
*{{cite journal |vauthors=Wu Y, Yoder A, Yu D |title=Cofilin activation in peripheral CD4 T cells of HIV-1 infected patients: a pilot study. |journal=Retrovirology |volume=5 |issue= 1|pages= 95 |year= 2008 |pmid= 18928553 |doi= 10.1186/1742-4690-5-95 |pmc=2576353 |display-authors=etal}} |
*{{cite journal |vauthors=Wu Y, Yoder A, Yu D |title=Cofilin activation in peripheral CD4 T cells of HIV-1 infected patients: a pilot study. |journal=Retrovirology |volume=5 |issue= 1|pages= 95 |year= 2008 |pmid= 18928553 |doi= 10.1186/1742-4690-5-95 |pmc=2576353 |display-authors=etal |doi-access=free }} |
||
*{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 |pmc=528928 |display-authors=etal}} |
*{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 |pmc=528928 |display-authors=etal}} |
||
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }} |
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }} |
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Latest revision as of 03:32, 3 December 2023
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | CFL2, NEM7, cofilin 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 601443; MGI: 101763; HomoloGene: 129115; GeneCards: CFL2; OMA:CFL2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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]
Function
[edit]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
[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.[11]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000165410 – Ensembl, May 2017
- ^ a b c 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)".
- ^ 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.
- ^ 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
[edit]- GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy
- Human CFL2 genome location and CFL2 gene details page in the UCSC Genome Browser.
Further reading
[edit]- 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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