Zyxina

ZYX
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB
Identificadores
Nomenclatura	Outros nomes ZYX, ESP-2, HED-2, zyxina ;
Símbolos	ZYX (HGNC: 13200) ZYX, ESP-2, HED-2, zyxina
Identificadores; externos	OMIM: 602002 ; MGI: 103072 ; HomoloGene: 31164 ; EBI: ZYX ; GeneCards: Xene ZYX ; UniProt: ZYX ;
Locus	Cr. 7 q34
Ontoloxía Xénica	Referencias: AmiGO / QuickGO
	Referencias: AmiGO / QuickGO
Ortólogos
Especies
Humano	Rato
Entrez
7791	22793
Ensembl
Véxase HS	Véxase MM
UniProt
Q15942	Q62523
RefSeq; (ARNm)
NM_001010972	NM_001289617
RefSeq; (proteína) NCBI
NP_001010972	NP_001276546
Localización (UCSC)
Cr. 7:; 143.38 – 143.39 Mb	Cr. 6:; 42.33 – 42.34 Mb
PubMed (Busca)
7791 ;	22793

A zyxina é unha proteína que nos humanos está codificada no xene ZYX do cromosoma 7.^[1]^[2]^[3]

Función

As adhesións focais son estruturas ricas en actina que permiten que as células se adhiran á matriz extracelular e á cal se ensamblan complexos proteicos implicados na transdución de sinais. A zyxina é unha fosfoproteína que se une ao zinc que se concentra nas adhesións focais e ao longo do citoesqueleto de actina. A zyxina ten un dominio rico en prolina N-terminal e tres dominios LIM na metade C-terminal. O dominio rico en prolina pode interaccionar cos dominios SH3 de proteínas implicados nas vías de transdución de sinais, mentres que os dominios LIM están probablemente implicados na unión proteína-proteína. A zyxina pode funcionar como un mensaxeiro na vía de transdución de sinais que media os cambios estimulados pola adhesión na expresión xénica e pode modular a organización citoesquelética de feixes de actina. O empalme alternativo orixina múltiples variantes de transcritos que codifican a mesma isoforma.^[3]

Interaccións

A zyxina presenta interaccións coas seguintes proteínas:

Actinina, alfa 1^[4]^[5]
ENAH,^[6]^[7]
LASP1,^[8]
LATS1,^[9] e
Fosfoproteína estimulada por vasodilatador.^[7]^[10]

Notas

↑ Zumbrunn J, Trueb B (xaneiro de 1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem 241 (2): 657–63. PMID 8917469. doi:10.1111/j.1432-1033.1996.00657.x.
↑ Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (xaneiro de 1997). "Molecular characterization of human zyxin". J Biol Chem 271 (49): 31470–8. PMID 8940160. doi:10.1074/jbc.271.49.31470.
1 2 "Entrez Gene: ZYX zyxin".
↑ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (maio de 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. doi:10.1074/jbc.274.19.13410.
↑ Li B, Trueb B (setembro de 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. PMID 11423549. doi:10.1074/jbc.M100789200.
↑ Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T (xuño de 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. PMID 12672821. doi:10.1074/jbc.M301447200.
1 2 Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (xullo de 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. PMID 10801818. doi:10.1074/jbc.M001698200.
↑ Li B, Zhuang L, Trueb B (maio de 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. PMID 15004028. doi:10.1074/jbc.M310304200.
↑ Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (maio de 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. PMC 2174824. PMID 10831611. doi:10.1083/jcb.149.5.1073.
↑ Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (outubro de 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. PMID 10882740. doi:10.1074/jbc.M005066200.

Véxase tamén

Bibliografía

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. PMC 41265. PMID 7644520. doi:10.1073/pnas.92.17.7956.
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. PMID 7696985.
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. PMID 8622875.
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. PMID 9367993. doi:10.1074/jbc.272.47.29407.
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. doi:10.1159/000015047.
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. PMID 9784834. doi:10.1080/15216549800203502.
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. PMID 10224105. doi:10.1074/jbc.274.19.13410.
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. PMID 10801818. doi:10.1074/jbc.M001698200.
Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (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. PMC 2174824. PMID 10831611. doi:10.1083/jcb.149.5.1073.
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. PMID 10851246. doi:10.1074/jbc.M909632199.
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. PMID 10882740. doi:10.1074/jbc.M005066200.
Schenker T, Trueb B (2000). "BSPRY, a novel protein of the Ro-Ret family". Biochim. Biophys. Acta 1493 (1–2): 255–8. PMID 10978534. doi:10.1016/s0167-4781(00)00167-6.
Li B, Trueb B (2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. PMID 11423549. doi:10.1074/jbc.M100789200.
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. PMC 114765. PMID 11689660. doi:10.1128/JVI.75.23.11791-11802.2001.
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. PMID 11782456. doi:10.1074/jbc.M106922200.
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. PMID 11841540. doi:10.1046/j.0022-202x.2001.01657.x.

Ligazóns externas

Zyxin Info with links in the Cell Migration Gateway Arquivado 11 de decembro de 2014 en Wayback Machine.

[pmid8917469-1] Zumbrunn J, Trueb B (xaneiro de 1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem 241 (2): 657–63. PMID 8917469. doi:10.1111/j.1432-1033.1996.00657.x.

[pmid8940160-2] Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (xaneiro de 1997). "Molecular characterization of human zyxin". J Biol Chem 271 (49): 31470–8. PMID 8940160. doi:10.1074/jbc.271.49.31470.

[entrez-3] 1 2 "Entrez Gene: ZYX zyxin".

[pmid10224105-4] Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (maio de 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. doi:10.1074/jbc.274.19.13410.

[pmid11423549-5] Li B, Trueb B (setembro de 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. PMID 11423549. doi:10.1074/jbc.M100789200.

[pmid12672821-6] Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T (xuño de 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. PMID 12672821. doi:10.1074/jbc.M301447200.

[pmid10801818-7] 1 2 Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (xullo de 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. PMID 10801818. doi:10.1074/jbc.M001698200.

[pmid15004028-8] Li B, Zhuang L, Trueb B (maio de 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. PMID 15004028. doi:10.1074/jbc.M310304200.

[pmid10831611-9] Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (maio de 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. PMC 2174824. PMID 10831611. doi:10.1083/jcb.149.5.1073.

[pmid10882740-10] Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (outubro de 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. PMID 10882740. doi:10.1074/jbc.M005066200.

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