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.[7]
^"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.
^Zumbrunn J, Trueb B (January 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. PMID8917469.
^Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (January 1997). "Molecular characterization of human zyxin". J Biol Chem. 271 (49): 31470–8. doi:10.1074/jbc.271.49.31470. PMID8940160.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^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. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID10224105.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T (June 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. doi:10.1074/jbc.M301447200. PMID12672821.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ abDrees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (July 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. PMID10801818.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Li B, Zhuang L, Trueb B (May 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. doi:10.1074/jbc.M310304200. PMID15004028.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Wang LF, Miao SY, Zong SD, Bai Y, Koide SS (1995). "Gene encoding a mammalian epididymal protein". Biochem. Mol. Biol. Int. 34 (6): 1131–6. PMID7696985.
Hobert O, Schilling JW, Beckerle MC, Ullrich A, Jallal B (1996). "SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin". Oncogene. 12 (7): 1577–81. PMID8622875.
Kotake K, Ozaki N, Mizuta M, Sekiya S, Inagaki N, Seino S (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. PMID9367993.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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. PMID9730620.
Yang JX, Miao SY, Wu YW, Zhang Z, Zong SD, Wang LF, Koide SS (1998). "Gene encoding a human testis Sertoli cell component related to LIM domain protein". Biochem. Mol. Biol. Int. 46 (1): 11–9. PMID9784834.
Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (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. PMID10224105.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (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. PMID10801818.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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. PMID10851246.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID10882740.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Yi J, Kloeker S, Jensen CC, Bockholt S, Honda H, Hirai H, Beckerle MC (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. PMID11782456.{{cite journal}}: CS1 maint: unflagged free DOI (link)
van der Gaag EJ, Leccia MT, Dekker SK, Jalbert NL, Amodeo DM, Byers HR (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. PMID11841540.