TRIO (gene)

From Wikipedia, the free encyclopedia

Triple functional domain (PTPRF interacting)

PDB rendering based on 1nty.

Available structures: 1nty, 2nz8

Identifiers

Symbol(s)

TRIO; tgat

External IDs

OMIM: 601893 MGI: 1927230 HomoloGene: 20847

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • guanyl-nucleotide exchange factor activity • Rho guanyl-nucleotide exchange factor activity • ATP binding • transferase activity
Cellular Component:	• intracellular
Biological Process:	• protein amino acid phosphorylation • transmembrane receptor protein tyrosine phosphatase signaling pathway • regulation of Rho protein signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_007118 (mRNA)
NP_009049 (protein)

XM_888341 (mRNA)
XP_893434 (protein)

Location

Chr 5: 14.2 - 14.56 Mb

Chr 15: 27.68 - 27.86 Mb

Pubmed search

[1]

[2]

Triple functional domain (PTPRF interacting), also known as TRIO, is a human gene.^[1]

[edit] References

^ Entrez Gene: TRIO triple functional domain (PTPRF interacting).

[edit] Further reading

Debant A, Serra-Pagès C, Seipel K, et al. (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. PMID 8643598.
Taviaux S, 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.
Liu X, 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.
Seipel K, 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 ( Pt 12): 1825–34. PMID 10341202.
Medley QG, 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. doi:10.1074/jbc.M003775200. PMID 10948190.
Bellanger JM, 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. doi:10.1038/35046533. PMID 11146652.
Gao Y, 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. doi:10.1074/jbc.M108865200. PMID 11595749.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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. doi:10.1074/jbc.M312677200. PMID 15199069.
Zheng M, 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. PMID 15215162.
Yoshizuka N, 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. doi:10.1074/jbc.M406082200. PMID 15308664.
Gerhard DS, 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. doi:10.1101/gr.2596504. PMID 15489334.
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. doi:10.1042/BC20050009. PMID 16033331.
Tao WA, 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. doi:10.1038/nmeth776. PMID 16094384.
Adamowicz M, 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. doi:10.1002/gcc.20343. PMID 16752383.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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. doi:10.1016/j.jmb.2007.02.060. PMID 17391702.
Rojas RJ, Yohe ME, Gershburg S, et al. (2007). "Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain.". J. Biol. Chem. 282 (40): 29201–10. doi:10.1074/jbc.M703458200. PMID 17606614.