Zyxin
Zyxin is a protein that in humans is encoded by the ZYX gene.[1][2][3]
Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.[3]
Interactions
Zyxin has been shown to interact with ENAH,[4][5] LASP1,[6] LATS1,[7] Actinin, alpha 1[8][9] and Vasodilator-stimulated phosphoprotein.[5][10]
References
- ^ Zumbrunn J, Trueb B (Jan 1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem 241 (2): 657–63. doi:10.1111/j.1432-1033.1996.00657.x. PMID 8917469.
- ^ Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (Jan 1997). "Molecular characterization of human zyxin". J Biol Chem 271 (49): 31470–8. doi:10.1074/jbc.271.49.31470. PMID 8940160.
- ^ a b "Entrez Gene: ZYX zyxin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7791.
- ^ Tani, Katsuko; Sato Seiichi, Sukezane Taiko, Kojima Hiroshi, Hirose Hidenori, Hanafusa Hidesaburo, Shishido Tomoyuki (Jun. 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. (United States) 278 (24): 21685–92. doi:10.1074/jbc.M301447200. ISSN 0021-9258. PMID 12672821.
- ^ a b Drees, B; Friederich E, Fradelizi J, Louvard D, Beckerle M C, Golsteyn R M (Jul. 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. (UNITED STATES) 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.
- ^ Li, Bo; Zhuang Lei, Trueb Beat (May. 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. (United States) 279 (19): 20401–10. doi:10.1074/jbc.M310304200. ISSN 0021-9258. PMID 15004028.
- ^ Hirota, T; Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (May. 2000). "Zyxin, a Regulator of Actin Filament Assembly, Targets the Mitotic Apparatus by Interacting with H-Warts/Lats1 Tumor Suppressor". J. Cell Biol. (UNITED STATES) 149 (5): 1073–86. doi:10.1083/jcb.149.5.1073. ISSN 0021-9525. PMC 2174824. PMID 10831611. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174824.
- ^ Reinhard, M; Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May. 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. (UNITED STATES) 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. ISSN 0021-9258. PMID 10224105.
- ^ Li, B; Trueb B (Sep. 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. (United States) 276 (36): 33328–35. doi:10.1074/jbc.M100789200. ISSN 0021-9258. PMID 11423549.
- ^ Harbeck, B; Hüttelmaier S, Schluter K, Jockusch B M, Illenberger S (Oct. 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. (UNITED STATES) 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
External links
Further reading
- Reinhard M, Jouvenal K, Tripier D, Walter U (1995). "Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7956–60. doi:10.1073/pnas.92.17.7956. PMC 41265. PMID 7644520. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41265.
- Wang LF, Miao SY, Zong SD et al. (1995). "Gene encoding a mammalian epididymal protein". Biochem. Mol. Biol. Int. 34 (6): 1131–6. PMID 7696985.
- Hobert O, Schilling JW, Beckerle MC et al. (1996). "SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin". Oncogene 12 (7): 1577–81. PMID 8622875.
- Kotake K, Ozaki N, Mizuta M et al. (1997). "Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells". J. Biol. Chem. 272 (47): 29407–10. doi:10.1074/jbc.272.47.29407. PMID 9367993.
- Zumbrunn J, Trueb B (1998). "Assignment of the ZYX gene for the LIM protein zyxin to human chromosome bands 7q34→q35 by in situ hybridization". Cytogenet. Cell Genet. 81 (3–4): 283–4. doi:10.1159/000015047. PMID 9730620.
- Yang JX, Miao SY, Wu YW et al. (1998). "Gene encoding a human testis Sertoli cell component related to LIM domain protein". Biochem. Mol. Biol. Int. 46 (1): 11–9. PMID 9784834.
- Reinhard M, Zumbrunn J, Jaquemar D et al. (1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105.
- Drees B, Friederich E, Fradelizi J et al. (2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
- Hirota T, Morisaki T, Nishiyama Y et al. (2000). "Zyxin, a Regulator of Actin Filament Assembly, Targets the Mitotic Apparatus by Interacting with H-Warts/Lats1 Tumor Suppressor". J. Cell Biol. 149 (5): 1073–86. doi:10.1083/jcb.149.5.1073. PMC 2174824. PMID 10831611. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174824.
- Smolenski A, Poller W, Walter U, Lohmann SM (2000). "Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I". J. Biol. Chem. 275 (33): 25723–32. doi:10.1074/jbc.M909632199. PMID 10851246.
- Harbeck B, Hüttelmaier S, Schluter K et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
- Schenker T, Trueb B (2000). "BSPRY, a novel protein of the Ro-Ret family". Biochim. Biophys. Acta 1493 (1–2): 255–8. PMID 10978534.
- Li B, Trueb B (2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549.
- Degenhardt YY, Silverstein S (2001). "Interaction of Zyxin, a Focal Adhesion Protein, with the E6 Protein from Human Papillomavirus Type 6 Results in Its Nuclear Translocation". J. Virol. 75 (23): 11791–802. doi:10.1128/JVI.75.23.11791-11802.2001. PMC 114765. PMID 11689660. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=114765.
- Yi J, Kloeker S, Jensen CC et al. (2002). "Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers". J. Biol. Chem. 277 (11): 9580–9. doi:10.1074/jbc.M106922200. PMID 11782456.
- van der Gaag EJ (2002). "Role of zyxin in differential cell spreading and proliferation of melanoma cells and melanocytes". J. Invest. Dermatol. 118 (2): 246–54. doi:10.1046/j.0022-202x.2001.01657.x. PMID 11841540.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Scherer SW, Cheung J, MacDonald JR et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2882961.