Zyxin

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Zyxin
Identifiers
Symbols ZYX ; ESP-2; HED-2
External IDs Template:OMIM5 Template:MGI HomoloGene31164
RNA expression pattern
File:PBB GE ZYX 200808 s at tn.png
File:PBB GE ZYX 215706 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Zyxin, also known as ZYX, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: ZYX zyxin".

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. PMID 7644520.
  • 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.
  • Zumbrunn J, Trueb B (1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur. J. Biochem. 241 (2): 657–63. PMID 8917469.
  • Macalma T, Otte J, Hensler ME; et al. (1997). "Molecular characterization of human zyxin". J. Biol. Chem. 271 (49): 31470–8. PMID 8940160.
  • 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. 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. 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. 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. PMID 10831611.
  • 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. PMID 11689660.
  • 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, Leccia MT, Dekker SK; et al. (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. PMID 12477932.
  • 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. PMID 12690205.

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