Biology:TRIO (gene)

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.

Interactions

TRIO (gene) has been shown to interact with Filamin and RHOA.

Further reading

• "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. 1997. doi:10.1159/000134524. PMID 9154137. 
• "NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio". Cell 95 (2): 269–77. Oct 1998. doi:10.1016/S0092-8674(00)81757-2. PMID 9790533. 
• "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. Jun 1999. doi:10.1242/jcs.112.12.1825. PMID 10341202. 
• "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. Nov 2000. doi:10.1074/jbc.M003775200. PMID 10948190. 
• "The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin". Nature Cell Biology 2 (12): 888–92. Dec 2000. doi:10.1038/35046533. PMID 11146652. 
• "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". The Journal of Biological Chemistry 276 (50): 47530–41. Dec 2001. doi:10.1074/jbc.M108865200. PMID 11595749. 
• "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. Sep 2004. doi:10.1074/jbc.M312677200. PMID 15199069. 
• "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. Jul 2004. doi:10.1016/S0002-9440(10)63275-0. PMID 15215162. 
• "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. Oct 2004. doi:10.1074/jbc.M406082200. PMID 15308664. 
• "Identification of novel neuronal isoforms of the Rho-GEF Trio". Biology of the Cell 98 (3): 183–93. Mar 2006. doi:10.1042/BC20050009. PMID 16033331. 
• "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods 2 (8): 591–8. Aug 2005. doi:10.1038/nmeth776. PMID 16094384. 
• "Frequent amplifications and abundant expression of TRIO, NKD2, and IRX2 in soft tissue sarcomas". Genes, Chromosomes & Cancer 45 (9): 829–38. Sep 2006. doi:10.1002/gcc.20343. PMID 16752383. 
• "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. Nov 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 
• "The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation". Journal of Molecular Biology 368 (5): 1307–20. May 2007. doi:10.1016/j.jmb.2007.02.060. PMID 17391702. 
• "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. Oct 2007. doi:10.1074/jbc.M703458200. 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.