TRIO (gene)

TRIO (gene)

Triple functional domain (PTPRF interacting), also known as TRIO, is a human gene.cite web | title = Entrez Gene: TRIO triple functional domain (PTPRF interacting)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7204| accessdate = ]

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References

Further reading

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*cite journal | author=Debant A, Serra-Pagès C, Seipel K, "et al." |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5466–71 |year= 1996 |pmid= 8643598 |doi=
*cite journal | author=Taviaux S, Diriong S, Bellanger JM, "et al." |title=Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=76 |issue= 1-2 |pages= 107–8 |year= 1997 |pmid= 9154137 |doi=
*cite journal | author=Liu X, Wang H, Eberstadt M, "et al." |title=NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. |journal=Cell |volume=95 |issue= 2 |pages= 269–77 |year= 1998 |pmid= 9790533 |doi=
*cite journal | author=Seipel K, Medley QG, Kedersha NL, "et al." |title=Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth. |journal=J. Cell. Sci. |volume=112 ( Pt 12) |issue= |pages= 1825–34 |year= 1999 |pmid= 10341202 |doi=
*cite journal | author=Medley QG, Serra-Pagès C, Iannotti E, "et al." |title=The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36116–23 |year= 2000 |pmid= 10948190 |doi= 10.1074/jbc.M003775200
*cite journal | author=Bellanger JM, Astier C, Sardet C, "et al." |title=The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin. |journal=Nat. Cell Biol. |volume=2 |issue= 12 |pages= 888–92 |year= 2001 |pmid= 11146652 |doi= 10.1038/35046533
*cite journal | author=Gao Y, Xing J, Streuli M, "et al." |title=Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47530–41 |year= 2002 |pmid= 11595749 |doi= 10.1074/jbc.M108865200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Skowronek KR, Guo F, Zheng Y, Nassar N |title=The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids. |journal=J. Biol. Chem. |volume=279 |issue= 36 |pages= 37895–907 |year= 2004 |pmid= 15199069 |doi= 10.1074/jbc.M312677200
*cite journal | author=Zheng M, Simon R, Mirlacher M, "et al." |title=TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer. |journal=Am. J. Pathol. |volume=165 |issue= 1 |pages= 63–9 |year= 2004 |pmid= 15215162 |doi=
*cite journal | author=Yoshizuka N, Moriuchi R, Mori T, "et al." |title=An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential. |journal=J. Biol. Chem. |volume=279 |issue= 42 |pages= 43998–4004 |year= 2004 |pmid= 15308664 |doi= 10.1074/jbc.M406082200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Portales-Casamar E, Briançon-Marjollet A, Fromont S, "et al." |title=Identification of novel neuronal isoforms of the Rho-GEF Trio. |journal=Biol. Cell |volume=98 |issue= 3 |pages= 183–93 |year= 2006 |pmid= 16033331 |doi= 10.1042/BC20050009
*cite journal | author=Tao WA, Wollscheid B, O'Brien R, "et al." |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591–8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776
*cite journal | author=Adamowicz M, Radlwimmer B, Rieker RJ, "et al." |title=Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas. |journal=Genes Chromosomes Cancer |volume=45 |issue= 9 |pages= 829–38 |year= 2006 |pmid= 16752383 |doi= 10.1002/gcc.20343
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026
*cite journal | author=Chhatriwala MK, Betts L, Worthylake DK, Sondek J |title=The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation. |journal=J. Mol. Biol. |volume=368 |issue= 5 |pages= 1307–20 |year= 2007 |pmid= 17391702 |doi= 10.1016/j.jmb.2007.02.060
*cite journal | author=Rojas RJ, Yohe ME, Gershburg S, "et al." |title=Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. |journal=J. Biol. Chem. |volume=282 |issue= 40 |pages= 29201–10 |year= 2007 |pmid= 17606614 |doi= 10.1074/jbc.M703458200

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