FLNA

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Template:Short description Script error: No such module "For". Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.[1][2]

Structure

The structure of filamin A, alpha includes an actin binding N terminal domain, 24 internal repeats and 2 hinge regions.[3][4]

Function

Actin-binding protein, or filamin, is a 280-kD protein that crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. Filamin A, encoded by the FLNA gene, is a widely expressed filamin that regulates the reorganization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes, and secondary messengers.[5] At least 31 disease-causing mutations in this gene have been discovered.[6]

DNA repair

Interaction of FLNA with the BRCA1 protein is required for efficient regulation of early stages of DNA repair processes.[7] FLNA is implicated in the control of the DNA repair process of homologous recombination and non-homologous end joining.[7]

Interactions

Filamin has been shown to interact with:

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References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Gorlin JB, Henske E, Warren ST, Kunst CB, D'Urso M, Palmieri G, et al. (October 1993). "Actin-binding protein (ABP-280) filamin gene (FLN) maps telomeric to the color vision locus (R/GCP) and centromeric to G6PD in Xq28". Genomics. 17 (2): 496–498. doi:10.1006/geno.1993.1354. PMID 8406501.
  2. ^ Page Module:Citation/CS1/styles.css has no content.Robertson SP, Twigg SR, Sutherland-Smith AJ, Biancalana V, Gorlin RJ, Horn D, et al. (March 2003). "Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans". Nature Genetics. 33 (4): 487–491. doi:10.1038/ng1119. PMID 12612583.
  3. ^ Page Module:Citation/CS1/styles.css has no content.Gräber P, Witt HT (February 1976). "Relations between the electrical potential, pH gradient, proton flux and phosphorylation in the photosynthetic membrane". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 423 (2): 141–163. doi:10.1016/0005-2728(76)90174-2. PMID 2316.
  4. ^ Page Module:Citation/CS1/styles.css has no content."P21333 (FLNA_HUMAN): Filamin-A". UniProt.
  5. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: FLNA filamin A, alpha (actin binding protein 280)".
  6. ^ Page Module:Citation/CS1/styles.css has no content.Šimčíková D, Heneberg P (December 2019). "Refinement of evolutionary medicine predictions based on clinical evidence for the manifestations of Mendelian diseases". Scientific Reports. 9 (1) 18577. Bibcode:2019NatSR...918577S. doi:10.1038/s41598-019-54976-4. PMC 6901466. PMID 31819097.
  7. ^ a b Page Module:Citation/CS1/styles.css has no content.Velkova A, Carvalho MA, Johnson JO, Tavtigian SV, Monteiro AN (April 2010). "Identification of Filamin A as a BRCA1-interacting protein required for efficient DNA repair". Cell Cycle. 9 (7). Georgetown, Tex.: 1421–1433. doi:10.4161/cc.9.7.11256. PMC 3040726. PMID 20305393.
  8. ^ Page Module:Citation/CS1/styles.css has no content.Yuan Y, Shen Z (December 2001). "Interaction with BRCA2 suggests a role for filamin-1 (hsFLNa) in DNA damage response". Journal of Biological Chemistry. 276 (51): 48318–48324. doi:10.1074/jbc.M102557200. PMID 11602572.
  9. ^ Page Module:Citation/CS1/styles.css has no content.van der Flier A, Kuikman I, Kramer D, Geerts D, Kreft M, Takafuta T, et al. (January 2002). "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits". The Journal of Cell Biology. 156 (2): 361–376. doi:10.1083/jcb.200103037. PMC 2199218. PMID 11807098.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Loo DT, Kanner SB, Aruffo A (September 1998). "Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction". Journal of Biological Chemistry. 273 (36): 23304–23312. doi:10.1074/jbc.273.36.23304. PMID 9722563.
  11. ^ Page Module:Citation/CS1/styles.css has no content.Hjälm G, MacLeod RJ, Kifor O, Chattopadhyay N, Brown EM (September 2001). "Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase". Journal of Biological Chemistry. 276 (37): 34880–34887. doi:10.1074/jbc.M100784200. PMID 11390380.
  12. ^ Page Module:Citation/CS1/styles.css has no content.Awata H, Huang C, Handlogten ME, Miller RT (September 2001). "Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein". Journal of Biological Chemistry. 276 (37): 34871–34879. doi:10.1074/jbc.M100775200. PMID 11390379.
  13. ^ Page Module:Citation/CS1/styles.css has no content.Tu Y, Wu S, Shi X, Chen K, Wu C (April 2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation". Cell. 113 (1): 37–47. doi:10.1016/s0092-8674(03)00163-6. PMID 12679033.
  14. ^ Page Module:Citation/CS1/styles.css has no content.Nagano T, Yoneda T, Hatanaka Y, Kubota C, Murakami F, Sato M (July 2002). "Filamin A-interacting protein (FILIP) regulates cortical cell migration out of the ventricular zone". Nature Cell Biology. 4 (7): 495–501. doi:10.1038/ncb808. PMID 12055638. S2CID 4795393.
  15. ^ Page Module:Citation/CS1/styles.css has no content.Sheen VL, Feng Y, Graham D, Takafuta T, Shapiro SS, Walsh CA (November 2002). "Filamin A and Filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact". Human Molecular Genetics. 11 (23): 2845–2854. doi:10.1093/hmg/11.23.2845. PMID 12393796.
  16. ^ Page Module:Citation/CS1/styles.css has no content.Donaldson JC, Dise RS, Ritchie MD, Hanks SK (August 2002). "Nephrocystin-conserved domains involved in targeting to epithelial cell-cell junctions, interaction with filamins, and establishing cell polarity". Journal of Biological Chemistry. 277 (32): 29028–29035. doi:10.1074/jbc.M111697200. PMID 12006559.
  17. ^ Page Module:Citation/CS1/styles.css has no content.Ohta Y, Suzuki N, Nakamura S, Hartwig JH, Stossel TP (March 1999). "The small GTPase RalA targets filamin to induce filopodia". Proceedings of the National Academy of Sciences of the United States of America. 96 (5): 2122–2128. Bibcode:1999PNAS...96.2122O. doi:10.1073/pnas.96.5.2122. PMC 26747. PMID 10051605.
  18. ^ Page Module:Citation/CS1/styles.css has no content.He X, Li Y, Schembri-King J, Jakes S, Hayashi J (August 2000). "Identification of actin binding protein, ABP-280, as a binding partner of human Lnk adaptor protein". Molecular Immunology. 37 (10): 603–612. doi:10.1016/s0161-5890(00)00070-5. PMID 11163396.
  19. ^ Page Module:Citation/CS1/styles.css has no content.Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A (December 2000). "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nature Cell Biology. 2 (12): 888–892. doi:10.1038/35046533. PMID 11146652. S2CID 10182923.
  20. ^ Page Module:Citation/CS1/styles.css has no content.Tsuchiya H, Iseda T, Hino O (July 1996). "Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product". Cancer Research. 56 (13): 2881–2885. PMID 8674032.
  21. ^ Page Module:Citation/CS1/styles.css has no content.Zhou MI, Wang H, Ross JJ, Kuzmin I, Xu C, Cohen HT (October 2002). "The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1". Journal of Biological Chemistry. 277 (42): 39887–39898. doi:10.1074/jbc.M205040200. PMID 12169691.

Further reading

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