コフィリン1、コフィリン-1
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/05/23 05:18:06」(JST)
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CFL1 |
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Available structures |
PDB |
Ortholog search: PDBe RCSB |
List of PDB id codes |
4BEX, 1Q8G, 1Q8X, 3J0S
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Identifiers |
Aliases |
CFL1, CFL, HEL-S-15, cofilin |
External IDs |
OMIM: 601442 MGI: 101757 HomoloGene: 99735 GeneCards: 1072 |
Gene ontology |
Molecular function |
• protein binding
• actin binding
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Cellular component |
• cytoplasm
• vesicle
• cell projection
• membrane
• cell-cell junction
• focal adhesion
• nuclear matrix
• plasma membrane
• intracellular
• ruffle membrane
• extracellular space
• cortical actin cytoskeleton
• actin cytoskeleton
• cytoskeleton
• lamellipodium membrane
• extracellular exosome
• cell nucleus
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Biological process |
• neural fold formation
• response to amino acid
• Fc-gamma receptor signaling pathway involved in phagocytosis
• actin filament organization
• ephrin receptor signaling pathway
• actin filament depolymerization
• mitotic cytokinesis
• response to virus
• platelet degranulation
• blood coagulation
• negative regulation of apoptotic process
• axon guidance
• platelet activation
• protein phosphorylation
• positive regulation by host of viral process
• cytoskeleton organization
• neural crest cell migration
• Rho protein signal transduction
• establishment of cell polarity
• regulation of cell morphogenesis
• innate immune response
• regulation of dendritic spine morphogenesis
• positive regulation of actin filament depolymerization
• actin cytoskeleton organization
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Sources:Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) |
Chr 11: 65.82 – 65.86 Mb |
Chr 19: 5.49 – 5.49 Mb |
PubMed search |
[1] |
[2] |
Wikidata |
View/Edit Human |
View/Edit Mouse |
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.[1]
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.[2][3]
Interactions
Cofilin 1 has been shown to interact with HSPH1[4] and LIMK1.[5][6]
References
- ^ "Entrez Gene: CFL1 cofilin 1 (non-muscle)".
- ^ Chai X, Förster E, Zhao S, Bock HH, Frotscher M (January 2009). "Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3". J. Neurosci. 29 (1): 288–99. doi:10.1523/JNEUROSCI.2934-08.2009. PMID 19129405.
- ^ Frotscher M, Chai X, Bock HH, Haas CA, Förster E, Zhao S (April 2009). "Role of Reelin in the development and maintenance of cortical lamination". J Neural Transm 116 (11): 1451–5. doi:10.1007/s00702-009-0228-7. PMID 19396394.
- ^ Saito Y, Doi K, Yamagishi N, Ishihara K, Hatayama T (Feb 2004). "Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems". Biochem. Biophys. Res. Commun. 314 (2): 396–402. doi:10.1016/j.bbrc.2003.12.108. PMID 14733918.
- ^ Foletta VC, Lim MA, Soosairajah J, Kelly AP, Stanley EG, Shannon M, He W, Das S, Massague J, Bernard O, Soosairaiah J (Sep 2003). "Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1". J. Cell Biol. 162 (6): 1089–98. doi:10.1083/jcb.200212060. PMC 2172847. PMID 12963706.
- ^ Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S (Aug 1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159.
Further reading
- 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.
- Samstag Y, Nebl G (2004). "Interaction of cofilin with the serine phosphatases PP1 and PP2A in normal and neoplastic human T lymphocytes". Adv. Enzyme Regul. 43: 197–211. doi:10.1016/S0065-2571(02)00031-6. PMID 12791392.
- Ogawa K, Tashima M, Yumoto Y, Okuda T, Sawada H, Okuma M, Maruyama Y (1991). "Coding sequence of human placenta cofilin cDNA". Nucleic Acids Res. 18 (23): 7169. doi:10.1093/nar/18.23.7169. PMC 332815. PMID 2263493.
- van der Steege G, Draaijers TG, Grootscholten PM, Osinga J, Anzevino R, Velonà I, Den Dunnen JT, Scheffer H, Brahe C, van Ommen GJ (1995). "A provisional transcript map of the spinal muscular atrophy (SMA) critical region". Eur. J. Hum. Genet. 3 (2): 87–95. PMID 7552146.
- Davidson MM, Haslam RJ (1994). "Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+". Biochem. J. 301 ( Pt 1) (Pt 1): 41–7. PMC 1137140. PMID 8037689.
- Ono S, Minami N, Abe H, Obinata T (1994). "Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle". J. Biol. Chem. 269 (21): 15280–6. PMID 8195165.
- Abe H, Nagaoka R, Obinata T (1993). "Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes". Exp. Cell Res. 206 (1): 1–10. doi:10.1006/excr.1993.1113. PMID 8482351.
- Gillett GT, Fox MF, Rowe PS, Casimir CM, Povey S (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.
- Okada K, Takano-Ohmuro H, Obinata T, Abe H (1996). "Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood". Exp. Cell Res. 227 (1): 116–22. doi:10.1006/excr.1996.0256. PMID 8806458.
- 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.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, Sowder RC, Chertova EN, Arthur LO, Henderson LE (1996). "Cytoskeletal proteins inside human immunodeficiency virus type 1 virions". J. Virol. 70 (11): 7734–43. PMC 190843. PMID 8892894.
- Yang N, Higuchi O, Ohashi K, Nagata K, Wada A, Kangawa K, Nishida E, Mizuno K (1998). "Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization". Nature 393 (6687): 809–12. doi:10.1038/31735. PMID 9655398.
- Rodal AA, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC (1999). "Aip1p Interacts with Cofilin to Disassemble Actin Filaments". J. Cell Biol. 145 (6): 1251–64. doi:10.1083/jcb.145.6.1251. PMC 2133144. PMID 10366597.
- Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S (1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159.
- Sumi T, Matsumoto K, Takai Y, Nakamura T (2000). "Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho- and Cdc42-Activated Lim-Kinase 2". J. Cell Biol. 147 (7): 1519–32. doi:10.1083/jcb.147.7.1519. PMC 2174243. PMID 10613909.
- Adachi R, Matsui S, Kinoshita M, Nagaishi K, Sasaki H, Kasahara T, Suzuki K (2001). "Nitric oxide induces chemotaxis of neutrophil-like HL-60 cells and translocation of cofilin to plasma membranes". Int. J. Immunopharmacol. 22 (11): 855–64. doi:10.1016/S0192-0561(00)00045-X. PMID 11090694.
- Lee K, Jung J, Kim M, Guidotti G (2001). "Interaction of the alpha subunit of Na,K-ATPase with cofilin". Biochem. J. 353 (Pt 2): 377–85. doi:10.1042/0264-6021:3530377. PMC 1221581. PMID 11139403.
- Toshima J, Toshima JY, Amano T, Yang N, Narumiya S, Mizuno K (2001). "Cofilin Phosphorylation by Protein Kinase Testicular Protein Kinase 1 and Its Role in Integrin-mediated Actin Reorganization and Focal Adhesion Formation". Mol. Biol. Cell 12 (4): 1131–45. doi:10.1091/mbc.12.4.1131. PMC 32292. PMID 11294912.
- Sumi T, Matsumoto K, Shibuya A, Nakamura T (2001). "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha". J. Biol. Chem. 276 (25): 23092–6. doi:10.1074/jbc.C100196200. PMID 11340065.
PDB gallery
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1q8g: NMR structure of human Cofilin
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1q8x: NMR structure of human cofilin
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Proteins of the cytoskeleton
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Human |
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Nonhuman |
- Major sperm proteins
- Prokaryotic cytoskeleton
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See also: cytoskeletal defects
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UpToDate Contents
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English Journal
- Enhanced docetaxel-mediated cytotoxicity in human prostate cancer cells through knockdown of cofilin-1 by carbon nanohorn delivered siRNA.
- Pérez-Martínez FC, Carrión B, Lucío MI, Rubio N, Herrero MA, Vázquez E, Ceña V.SourceNanoDrugs, S.L. Parque Científico y Tecnológico, 02071 Albacete, Spain.
- Biomaterials.Biomaterials.2012 Nov;33(32):8152-9. doi: 10.1016/j.biomaterials.2012.07.038. Epub 2012 Aug 2.
- We synthesized a non-viral delivery system (f-CNH3) for small interfering RNA (siRNA) by anchoring a fourth-generation polyamidoamine dendrimer (G4-PAMAM) to carbon nanohorns (CNHs). Using this new compound, we delivered a specific siRNA designed to knockdown cofilin-1, a key protein in the regulati
- PMID 22858003
- Adipose tissue proteomes of intrauterine growth-restricted piglets artificially reared on a high-protein neonatal formula.
- Sarr O, Louveau I, Le Huërou-Luron I, Gondret F.SourceINRA, UMR1079 Systèmes d'Elevage Nutrition Animale et Humaine, F-35590 Saint-Gilles, France; Agrocampus Ouest, UMR1079 Systèmes d'Elevage Nutrition Animale et Humaine, F-35000 Rennes, France.
- The Journal of nutritional biochemistry.J Nutr Biochem.2012 Nov;23(11):1417-24. doi: 10.1016/j.jnutbio.2011.09.002. Epub 2012 Jan 4.
- The eventuality that adipose tissues adapt to neonatal nutrition in a way that may program later adiposity or obesity in adulthood is receiving increasing attention in neonatology. This study assessed the immediate effects of a high-protein neonatal formula on proteome profiles of adipose tissues in
- PMID 22221677
Japanese Journal
- Synergistic action of dendritic mitochondria and creatine kinase maintains ATP homeostasis and actin dynamics in growing neuronal dendrites.
- Fukumitsu Kansai,Fujishima Kazuto,Yoshimura Azumi,Wu You Kure,Heuser John,Kengaku Mineko
- The Journal of neuroscience : the official journal of the Society for Neuroscience 35(14), 5707-5723, 2015-04-08
- … Mechanistically, this energy depletion appears to perturb normal actin dynamics and enhance the aggregation of cofilin within growing dendrites, reminiscent of what occurs in neurons overexpressing the dephosphorylated form of cofilin. …
- NAID 120005593705
- Cofilin-1 is involved in regulation of actin reorganization during influenza A virus assembly and budding
- Liu Ge,Xiang Yangfei,Guo Chaowan,Pei Ying,Wang Yifei,Kitazato Kaio
- Biochemical and Biophysical Research Communications 453(4), 821-825, 2014-10-31
- … In this study, we found that the natural antiviral compound petagalloyl glucose (PGG) inhibits F-actin reorganization in the host cell membrane during the late stage of IAV infection, which are associated with the suppression of total cofilin-1 level and its phosphorylation. … Knock-down of cofilin-1 reduces viral yields. … These findings provide the first evidence that cofilin-1 plays an important role in regulating actin reorganization during IAV assembly and budding. …
- NAID 120005522353
- Gabapentin Prevents Oxaliplatin-Induced Mechanical Hyperalgesia in Mice
- Ohsawa Masahiro,Otake Saki,Murakami Tomoyasu [他]
- Journal of pharmacological sciences 125(3), 292-299, 2014-07
- NAID 40020129308
Related Links
- Cofilin 1 (non-muscle; n-cofilin), also known as CFL1, is a human gene, part of the ADF/cofilin family. Cofilin is a ... One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the ...
- Function. Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology ...
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- cofilin 1
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コフィリン
- 関
- actin depolymerizing factor