Filamin C, gamma (actin binding protein 280), also known as FLNC, is a human gene. The Human Genome Organisation (HUGO is an organization involved in the Human Genome Project, a project about mapping the human genome The Mouse Genome Informatics (MGI website is run by The Jackson Laboratory. HomoloGene, a tool of the National Center for Biotechnology Information (NCBI is a system for automated detection of homologs (similarity attributable to descent The Entrez Global Query Cross-Database Search System is a powerful Federated search engine or Web portal that allows users to search many discrete Health sciences Ensembl is a joint scientific project between the European Bioinformatics Institute and the Wellcome Trust Sanger Institute, which was launched in 1999 in response to the imminent UniProt is the uni versal prot ein resource a central repository of Protein data created by combining Swiss-Prot, TrEMBL PubMed is a free search engine for accessing the MEDLINE database of citations and abstracts of biomedical research articles History See also History of genetics The existence of genes was first suggested by Gregor Mendel (1822-1884 who in the 1860s studied inheritance [1]
This gene encodes one of three related filamin genes, specifically gamma filamin. These filamin proteins crosslink actin filaments into orthogonal networks in cortical cytoplasm and participate in the anchoring of membrane proteins for the actin cytoskeleton. Three functional domains exist in filamin: an N-terminal filamentous actin-binding domain, a C-terminal self-association domain, and a membrane glycoprotein-binding domain. [1]
References
Further reading
- Stossel TP, Condeelis J, Cooley L, et al. (2001). "Filamins as integrators of cell mechanics and signalling. ". Nat. Rev. Mol. Cell Biol. 2 (2): 138–45. doi:10.1038/35052082. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 11252955.
- Maestrini E, Patrosso C, Mancini M, et al. (1993). "Mapping of two genes encoding isoforms of the actin binding protein ABP-280, a dystrophin like protein, to Xq28 and to chromosome 7. ". Hum. Mol. Genet. 2 (6): 761–6. PMID 7689010.
- Gariboldi M, Maestrini E, Canzian F, et al. (1994). "Comparative mapping of the actin-binding protein 280 genes in human and mouse. ". Genomics 21 (2): 428–30. PMID 8088838.
- Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization. ". Genome Res. 6 (1): 35–42. PMID 8681137.
- Marti A, Luo Z, Cunningham C, et al. (1997). "Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells. ". J. Biol. Chem. 272 (5): 2620–8. PMID 9006895.
- Liu G, Thomas L, Warren RA, et al. (1998). "Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway. ". J. Cell Biol. 139 (7): 1719–33. PMID 9412467.
- Xu W, Xie Z, Chung DW, Davie EW (1998). "A novel human actin-binding protein homologue that binds to platelet glycoprotein Ibalpha. ". Blood 92 (4): 1268–76. PMID 9694715.
- Xie Z, Xu W, Davie EW, Chung DW (1998). "Molecular cloning of human ABPL, an actin-binding protein homologue. ". Biochem. Biophys. Res. Commun. 251 (3): 914–9. PMID 9791010.
- Thompson TG, Chan YM, Hack AA, et al. (2000). "Filamin 2 (FLN2): A muscle-specific sarcoglycan interacting protein. ". J. Cell Biol. 148 (1): 115–26. PMID 10629222.
- van der Ven PF, Obermann WM, Lemke B, et al. (2000). "Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation. ". Cell Motil. Cytoskeleton 45 (2): 149–62. doi:10.1002/(SICI)1097-0169(200002)45:2<149::AID-CM6>3.0.CO;2-G. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 10658210.
- Faulkner G, Pallavicini A, Comelli A, et al. (2001). "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. ". J. Biol. Chem. 275 (52): 41234–42. doi:10.1074/jbc.M007493200. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 10984498.
- van der Ven PF, Wiesner S, Salmikangas P, et al. (2000). "Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin. ". J. Cell Biol. 151 (2): 235–48. PMID 11038172.
- Petrecca K, Miller DM, Shrier A (2001). "Localization and enhanced current density of the Kv4. 2 potassium channel by interaction with the actin-binding protein filamin. ". J. Neurosci. 20 (23): 8736–44. PMID 11102480.
- Chakarova C, Wehnert MS, Uhl K, et al. (2001). "Genomic structure and fine mapping of the two human filamin gene paralogues FLNB and FLNC and comparative analysis of the filamin gene family. ". Hum. Genet. 107 (6): 597–611. PMID 11153914.
- Takada F, Vander Woude DL, Tong HQ, et al. (2001). "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines. ". Proc. Natl. Acad. Sci. U. S. A. 98 (4): 1595–600. doi:10.1073/pnas.041609698. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 11171996.
- Dyson JM, O'Malley CJ, Becanovic J, et al. (2002). "The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. ". J. Cell Biol. 155 (6): 1065–79. doi:10.1083/jcb.200104005. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 11739414.
- Frey N, Olson EN (2002). "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. ". J. Biol. Chem. 277 (16): 13998–4004. doi:10.1074/jbc.M200712200. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 11842093.
- Donaldson JC, Dise RS, Ritchie MD, Hanks SK (2002). "Nephrocystin-conserved domains involved in targeting to epithelial cell-cell junctions, interaction with filamins, and establishing cell polarity. ". J. Biol. Chem. 277 (32): 29028–35. doi:10.1074/jbc.M111697200. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 12006559.
- Shoeman RL, Hartig R, Hauses C, Traub P (2003). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. ". Cell Biol. Int. 26 (6): 529–39. PMID 12119179.
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