TRIO (gene)

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	n/a
	Wikidata
View/Edit Human

The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.

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

↑ 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.
↑ "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.
↑ 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.
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.

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

[pmid8643598-1] 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.

[entrez-2] "Entrez Gene: TRIO triple functional domain (PTPRF interacting)".

[pmid11146652-3] 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.

[pmid10948190-4] 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.

[1]

[2]

[3]

[4]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme 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)

TRIO (gene)

Interactions

References

Further reading

Navigation menu