Zyxin

From Wikipedia, the free encyclopedia

Zyxin

Identifiers

ZYX; ESP-2; HED-2

External IDs

OMIM: 602002 MGI: 103072 HomoloGene: 31164

Gene ontology
Molecular Function:	• protein binding • zinc ion binding • metal ion binding
Cellular Component:	• plasma membrane • integral to plasma membrane • cell-cell adherens junction
Biological Process:	• cell adhesion • signal transduction • cell-cell signaling

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001010972 (mRNA)
NP_001010972 (protein)

NM_011777 (mRNA)
NP_035907 (protein)

Location

Chr 7: 142.79 - 142.8 Mb

Chr 6: 42.28 - 42.29 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: ZYX zyxin.

[edit] 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.