TRIO (gen)

Faktor razmene trio ro guanina
Faktor razmene trio ro guanina
	PDB prikaz baziran na 1nty.
Dostupne strukture
	1NTY, 2NZ8
Identifikatori
Simboli	TRIO; ARHGEF23; tgat
Vanjski ID	OMIM: 601893 MGI: 1927230 HomoloGene: 20847 GeneCards: TRIO Gene
EC broj	2.7.11.1
Ontologija gena
Molekularna funkcija	• aktivnost proteinske serin/treoninske kinaze; • aktivnost faktora guanil-nukleotidne razmene; • aktivnost faktora ro guanil-nukleotidne razmene;
Celularna komponenta	• citozol;
Biološki proces	• apoptotički proces; • signalni put transmembranskog receptora protein tirozinske fosfataze; • prenos signala posredovan malom GTPazom; • aksonsko vođenje;
Pregled RNK izražavanja
	podaci
Ortolozi
Vrsta	Čovek
Entrez	7204
Ensembl	ENSG00000038382
UniProt	O75962
RefSeq (mRNA)	NM_007118.2
RefSeq (protein)	NP_009049.2
Lokacija (UCSC)	Chr 5:; 14.14 - 14.53 Mb
PubMed pretraga	[1]

Protein trofunkcionog domena (engl. Triple functional domain protein) je protein koji je kod ljudi kodiran TRIO genom.^[1]^[2]

Interakcije uredi

TRIO (gen) formira interakcije sa filaminom^[3] i RHOA.^[4]

Reference uredi

^ Debant A, Serra-Pages C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M (1996). „The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains”. Proc Natl Acad Sci U S A. 93 (11): 5466—71. PMC 39269  . PMID 8643598. doi:10.1073/pnas.93.11.5466.
^ „Entrez Gene: TRIO triple functional domain (PTPRF interacting)”.
^ Bellanger, J M; C, Astier; et al. (2000). „The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin”. Nat. Cell Biol. ENGLAND. 2 (12): 888—92. ISSN 1465-7392. PMID 11146652. doi:10.1038/35046533.
^ Medley, Q G; Serra-Pagès C; et al. (2000). „The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain”. J. Biol. Chem. UNITED STATES. 275 (46): 36116—23. ISSN 0021-9258. PMID 10948190. doi:10.1074/jbc.M003775200.

Literatura uredi

S, Taviaux; Diriong S; Bellanger JM; et al. (1997). „Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization”. Cytogenet. Cell Genet. 76 (1–2): 107—8. PMID 9154137. doi:10.1159/000134524.
X, Liu; Wang H; Eberstadt M; et al. (1998). „NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio”. Cell. 95 (2): 269—77. PMID 9790533. doi:10.1016/S0092-8674(00)81757-2.
K, Seipel; Medley QG; Kedersha NL; et al. (1999). „Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth”. J. Cell. Sci. 112 (12): 1825—34. PMID 10341202.
QG, Medley; Serra-Pagès C; Iannotti E; et al. (2000). „The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain”. J. Biol. Chem. 275 (46): 36116—23. PMID 10948190. doi:10.1074/jbc.M003775200.
JM, Bellanger; Astier C; Sardet C; et al. (2001). „The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin”. Nat. Cell Biol. 2 (12): 888—92. PMID 11146652. doi:10.1038/35046533.
Y, Gao; Xing J; Streuli M; et al. (2002). „Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors”. J. Biol. Chem. 276 (50): 47530—41. PMID 11595749. doi:10.1074/jbc.M108865200.
RL, Strausberg; 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. PMC 139241  . PMID 12477932. doi:10.1073/pnas.242603899.
T, Ota; Suzuki Y; Nishikawa T; et al. (2004). „Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40—5. PMID 14702039. doi:10.1038/ng1285.
Skowronek KR, Guo F, Zheng Y, Nassar N (2004). „The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids”. J. Biol. Chem. 279 (36): 37895—907. PMID 15199069. doi:10.1074/jbc.M312677200.
M, Zheng; Simon R; Mirlacher M; et al. (2004). „TRIO Amplification and Abundant mRNA Expression Is Associated with Invasive Tumor Growth and Rapid Tumor Cell Proliferation in Urinary Bladder Cancer”. Am. J. Pathol. 165 (1): 63—9. PMC 1618551  . PMID 15215162. doi:10.1016/S0002-9440(10)63275-0.
N, Yoshizuka; Moriuchi R; Mori T; et al. (2004). „An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential”. J. Biol. Chem. 279 (42): 43998—4004. PMID 15308664. doi:10.1074/jbc.M406082200.
DS, Gerhard; Wagner L; Feingold EA; et al. (2004). „The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121—7. PMC 528928  . PMID 15489334. doi:10.1101/gr.2596504.
Portales-Casamar E; Briançon-Marjollet A; Fromont S; et al. (2006). „Identification of novel neuronal isoforms of the Rho-GEF Trio”. Biol. Cell. 98 (3): 183—93. PMID 16033331. doi:10.1042/BC20050009.
WA, Tao; Wollscheid B; O'Brien R; et al. (2005). „Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry”. Nat. Methods. 2 (8): 591—8. PMID 16094384. doi:10.1038/nmeth776.
M, Adamowicz; Radlwimmer B; Rieker RJ; et al. (2006). „Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas”. Genes Chromosomes Cancer. 45 (9): 829—38. PMID 16752383. doi:10.1002/gcc.20343.
JV, Olsen; Blagoev B; Gnad F; et al. (2006). „Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635—48. PMID 17081983. doi:10.1016/j.cell.2006.09.026.
Chhatriwala MK, Betts L, Worthylake DK, Sondek J (2007). „The DH and PH Domains of Trio Coordinately Engage Rho GTPases for their Efficient Activation”. J. Mol. Biol. 368 (5): 1307—20. PMC 1890047  . PMID 17391702. doi:10.1016/j.jmb.2007.02.060.
RJ, Rojas; Yohe ME; Gershburg S; et al. (2007). „Gαq Directly Activates p63RhoGEF and Trio via a Conserved Extension of the Dbl Homology-associated Pleckstrin Homology Domain”. J. Biol. Chem. 282 (40): 29201—10. PMC 2655113  . PMID 17606614. doi:10.1074/jbc.M703458200.

[pmid8643598-1] Debant A, Serra-Pages C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M (1996). „The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains”. Proc Natl Acad Sci U S A. 93 (11): 5466—71. PMC 39269  . PMID 8643598. doi:10.1073/pnas.93.11.5466.

[entrez-2] „Entrez Gene: TRIO triple functional domain (PTPRF interacting)”.

[pmid11146652-3] Bellanger, J M; C, Astier; et al. (2000). „The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin”. Nat. Cell Biol. ENGLAND. 2 (12): 888—92. ISSN 1465-7392. PMID 11146652. doi:10.1038/35046533.

[pmid10948190-4] Medley, Q G; Serra-Pagès C; et al. (2000). „The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain”. J. Biol. Chem. UNITED STATES. 275 (46): 36116—23. ISSN 0021-9258. PMID 10948190. doi:10.1074/jbc.M003775200.

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