TRIO (gene)

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, TRIO gene
External IDs	OMIM: 601893; MGI: 1927230; HomoloGene: 20847; GeneCards: TRIO; OMA:TRIO - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	14,532,128 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	28,025,934 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; stromal cell of endometrium; ; gastric mucosa; ; ganglionic eminence; ; Achilles tendon; ; ascending aorta; ; transverse colon; ; left coronary artery; ; upper lobe of left lung; ; gallbladder;
	Top expressed in
	superior frontal gyrus; ; cerebellar cortex; ; internal carotid artery; ; lateral geniculate nucleus; ; ventromedial nucleus; ; external carotid artery; ; olfactory bulb; ; cerebellar vermis; ; subiculum; ; vas deferens;
	More reference expression data
	; ; ; ;
	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; protein binding; ATP binding;
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
	7204
	223435
	ENSG00000038382
	ENSMUSG00000022263
	O75962
	Q0KL02
	NM_007118
	NM_001081302
	NP_009049
	NP_001074771
	Wikidata
View/Edit Human	View/Edit Mouse

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

Interactions

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000038382 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022263 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1996PNAS...93.5466D. doi:10.1073/pnas.93.11.5466. PMC 39269. PMID 8643598.
^ "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".
^ 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.
^ 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.

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. doi:10.1242/jcs.112.12.1825. 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.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000038382 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8643598-5] 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. Bibcode:1996PNAS...93.5466D. doi:10.1073/pnas.93.11.5466. PMC 39269. PMID 8643598.

[entrez-6] "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".

[pmid11146652-7] 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.

[pmid10948190-8] 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.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Interactions

References

Further reading

External links