TRIO (gene)

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.[5][6]

TRIO
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1NTY, 2NZ8
Identifiers
Aliases	TRIO, ARHGEF23, tgat, trio Rho guanine nucleotide exchange factor, MEBAS, MRD44, MRD63
External IDs	OMIM: 601893 MGI: 1927230 HomoloGene: 20847 GeneCards: TRIO
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5p15.2 Start 14,143,342 bp[1] End 14,532,128 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 B1 Start 27,730,651 bp[2] End 28,025,848 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • guanyl-nucleotide exchange factor activity • kinase activity • protein serine/threonine kinase activity • GO:0001948 protein binding • ATP binding • Rho guanyl-nucleotide exchange factor activity Cellular component • cytoplasm • cytosol Biological process • phosphorylation • protein phosphorylation • transmembrane receptor protein tyrosine phosphatase signaling pathway • positive regulation of apoptotic process • regulation of Rho protein signal transduction • regulation of small GTPase mediated signal transduction • negative regulation of fat cell differentiation • G-protein coupled receptor signaling pathway • axon guidance • central nervous system development Sources:Amigo / QuickGO
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	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

TRIO (gene) has been shown to interact with Filamin[7] and RHOA.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000038382 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022263 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".
7. 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. S2CID 10182923.
8. 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. S2CID 18146575.
• 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. S2CID 10182923.
• 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. 98 (3): 183–93. doi:10.1042/BC20050009. PMID 16033331. S2CID 24166861.
• 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. S2CID 20475874.
• 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. S2CID 24491021.
• 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. S2CID 7827573.
• 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.

External links

• Overview of all the structural information available in the PDB for UniProt: O75962 (Triple functional domain protein) at the PDBe-KB.