Zyxin

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ZYX
Identifiers
Aliases ZYX, ESP-2, HED-2, zyxin
External IDs MGI: 103072 HomoloGene: 31164 GeneCards: ZYX
RNA expression pattern
PBB GE ZYX 215706 x at fs.png

PBB GE ZYX 200808 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001010972
NM_003461

NM_001289617
NM_001289618
NM_001289619
NM_011777

RefSeq (protein)

NP_001010972
NP_003452

Location (UCSC) Chr 7: 143.38 – 143.39 Mb Chr 6: 42.35 – 42.36 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Zyxin is a protein that in humans is encoded by the ZYX gene.[3][4][5]

Function[edit]

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.[5]

Interactions[edit]

Zyxin has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. PMID 8917469. 
  4. ^ 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. PMID 8940160. 
  5. ^ a b "Entrez Gene: ZYX zyxin". 
  6. ^ 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. PMID 10224105. 
  7. ^ Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549. 
  8. ^ 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. PMID 12672821. 
  9. ^ a b Drees 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. PMID 10801818. 
  10. ^ 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. PMID 15004028. 
  11. ^ 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. 149 (5): 1073–86. doi:10.1083/jcb.149.5.1073. PMC 2174824Freely accessible. PMID 10831611. 
  12. ^ Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 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. 

Further reading[edit]

External links[edit]