TRIO (gene)

Trio Rho guanine nucleotide exchange factor
PDB rendering based on 1nty.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1NTY​, 2NZ8​
Identifiers
Symbols	TRIO ; ARHGEF23; tgat
External IDs	OMIM: 601893 MGI: 1927230 HomoloGene: 20847 GeneCards: TRIO Gene
EC number	2.7.11.1
Gene ontology Molecular function • protein serine/threonine kinase activity • guanyl-nucleotide exchange factor activity • Rho guanyl-nucleotide exchange factor activity • protein binding • ATP binding • enzyme binding Cellular component • cytosol Biological process • protein phosphorylation • transmembrane receptor protein tyrosine phosphatase signaling pathway • small GTPase mediated signal transduction • axon guidance • regulation of Rho protein signal transduction • positive regulation of apoptotic process • positive regulation of GTPase activity • neurotrophin TRK receptor signaling pathway • regulation of small GTPase mediated signal transduction • apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7204	223435
Ensembl	ENSG00000038382	ENSMUSG00000022263
UniProt	O75962	Q0KL02
RefSeq (mRNA)	NM_007118	NM_001081302
RefSeq (protein)	NP_009049	NP_001074771
Location (UCSC)	Chr 5: 14.14 – 14.53 Mb	Chr 15: 27.73 – 28.03 Mb
PubMed search

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.^[1][2]

Interactions

TRIO (gene) has been shown to interact with Filamin^[3] and RHOA.^[4]

References

1. Debant A, Serra-Pagès C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M (May 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". Proceedings of the National Academy of Sciences of the United States of America 93 (11): 5466–71. doi:10.1073/pnas.93.11.5466. PMC 39269. PMID 8643598.
2. "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".
3. Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A (Dec 2000). "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nature Cell Biology 2 (12): 888–92. doi:10.1038/35046533. PMID 11146652.
4. Medley QG, Serra-Pagès C, Iannotti E, Seipel K, Tang M, O'Brien SP, Streuli M (Nov 2000). "The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain". The Journal of Biological Chemistry 275 (46): 36116–23. doi:10.1074/jbc.M003775200. PMID 10948190.

Further reading

• Taviaux S, Diriong S, Bellanger JM, Streuli M, Debant A (1997). "Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization". Cytogenetics and Cell Genetics 76 (1-2): 107–8. doi:10.1159/000134524. PMID 9154137.
• Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW (Oct 1998). "NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio". Cell 95 (2): 269–77. doi:10.1016/S0092-8674(00)81757-2. PMID 9790533.
• Seipel K, Medley QG, Kedersha NL, Zhang XA, O'Brien SP, Serra-Pages C, Hemler ME, Streuli M (Jun 1999). "Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth". Journal of Cell Science. 112 ( Pt 12) (12): 1825–34. PMID 10341202.
• Medley QG, Serra-Pagès C, Iannotti E, Seipel K, Tang M, O'Brien SP, Streuli M (Nov 2000). "The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain". The Journal of Biological Chemistry 275 (46): 36116–23. doi:10.1074/jbc.M003775200. PMID 10948190.
• Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, Debant A (Dec 2000). "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nature Cell Biology 2 (12): 888–92. doi:10.1038/35046533. PMID 11146652.
• Gao Y, Xing J, Streuli M, Leto TL, Zheng Y (Dec 2001). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". The Journal of Biological Chemistry 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.
• Skowronek KR, Guo F, Zheng Y, Nassar N (Sep 2004). "The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids". The Journal of Biological Chemistry 279 (36): 37895–907. doi:10.1074/jbc.M312677200. PMID 15199069.
• Zheng M, Simon R, Mirlacher M, Maurer R, Gasser T, Forster T, Diener PA, Mihatsch MJ, Sauter G, Schraml P (Jul 2004). "TRIO amplification and abundant mRNA expression is associated with invasive tumor growth and rapid tumor cell proliferation in urinary bladder cancer". The American Journal of Pathology 165 (1): 63–9. doi:10.1016/S0002-9440(10)63275-0. PMC 1618551. PMID 15215162.
• Yoshizuka N, Moriuchi R, Mori T, Yamada K, Hasegawa S, Maeda T, Shimada T, Yamada Y, Kamihira S, Tomonaga M, Katamine S (Oct 2004). "An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential". The Journal of Biological Chemistry 279 (42): 43998–4004. doi:10.1074/jbc.M406082200. PMID 15308664.
• Portales-Casamar E, Briançon-Marjollet A, Fromont S, Triboulet R, Debant A (Mar 2006). "Identification of novel neuronal isoforms of the Rho-GEF Trio". Biology of the Cell / Under the Auspices of the European Cell Biology Organization 98 (3): 183–93. doi:10.1042/BC20050009. PMID 16033331.
• Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (Aug 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
• Adamowicz M, Radlwimmer B, Rieker RJ, Mertens D, Schwarzbach M, Schraml P, Benner A, Lichter P, Mechtersheimer G, Joos S (Sep 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, Macek B, Kumar C, Mortensen P, Mann M (Nov 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 (May 2007). "The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation". Journal of Molecular Biology 368 (5): 1307–20. doi:10.1016/j.jmb.2007.02.060. PMC 1890047. PMID 17391702.
• Rojas RJ, Yohe ME, Gershburg S, Kawano T, Kozasa T, Sondek J (Oct 2007). "Galphaq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain". The Journal of Biological Chemistry 282 (40): 29201–10. doi:10.1074/jbc.M703458200. PMC 2655113. PMID 17606614.