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TRIO  -  trio Rho guanine nucleotide exchange factor

Homo sapiens

 
 
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Disease relevance of TRIO

  • Three commercially available systems, the 4-h Minitek Enterobacteriaceae III, the Haemophilus Trio-Tube, and the Micro-ID, were evaluated for their capacities to identify and biotype 308 respiratory isolates of Haemophilus spp [1].
  • A selective medium was incorporated into a new three-media dipslide (Uricult Trio, Orion Diagnostica) to allow rapid identification of Escherichia coli [2].
  • CONCLUSION: Uricult Trio is not effective as a screening test for asymptomatic bacteriuria in pregnancy or for diagnosing UTIs in women with symptoms suggestive of infection [3].
  • MATERIAL AND METHODS: Seven volunteers and 5 patients (4 aneurysms, 1 AVM) underwent 3D-ToF-MRA at 1.5T (Magnetom Sonata) and 3.0T (Magnetom Trio) with and without parallel acquisition techniques (iPAT) using similarly designed 8-channel phased-array head coils [4].
 

High impact information on TRIO

  • Here we describe the solution structure of the N-terminal DH domain of Trio that catalyzes nucleotide exchange for Rac1 [5].
  • NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio [5].
  • Here we show that Trio GEFD1 interacts through its PH domain with the actin-filament-crosslinking protein filamin, and localizes with endogenous filamin in HeLa cells [6].
  • 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 [7].
  • Northern blot analysis indicates that Trio has a broad tissue distribution [7].
 

Biological context of TRIO

  • Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization [8].
  • Genetic analyses in Drosophila and in Caenorhabditis elegans indicate that Trio is involved in axon guidance and cell motility via a GEFD1-dependent process, suggesting that the activity of its Rho-GEFs is strictly regulated [9].
  • Sequence comparison revealed that an alternative RNA splicing of the Trio gene was involved in the generation of Tgat [10].
  • The Tgat cDNA encoded a protein product consisting of the Rho-guanosine nucleotide exchange factor (GEF) domain of a multifunctional protein, TRIO, and a unique C-terminal 15-amino acid sequence, which were derived from the exons 38-46 of the Trio gene and a novel exon located downstream of its last exon (exon 58), respectively [10].
  • Trio is essential for mouse embryonic development and Trio-deficiency is associated with abnormal skeletal muscle and neural tissue development [11].
 

Anatomical context of TRIO

  • Here, we show that human Trio induces neurite outgrowth in PC12 cells in a GEFD1-dependent manner [9].
  • It readily blocked the platelet-derived growth factor (PDGF)-induced lamellipodia formation and inhibited the wild type Trio-induced serum response factor activation [12].
  • Expression of full-length Trio in COS cells also alters actin cytoskeleton organization, as well as the distribution of focal contact sites [13].
  • To assess the functional role of the two Trio guanine nucleotide exchange factor domains, NIH 3T3 cell lines stably expressing the individual guanine nucleotide exchange factor domains were established and characterized [13].
  • Solo/Trio8, a membrane-associated short isoform of Trio, modulates endosome dynamics and neurite elongation [14].
 

Associations of TRIO with chemical compounds

  • Trio appears to be phosphorylated only on serine residues, suggesting that Trio is not a LAR substrate, but rather that it forms a complex with LAR [7].
  • Our data suggest a role for the phosphoinositide 3-kinase, PI 3-kinase, in modulating the Trio/RhoG signaling pathway [15].
  • When sucrose was added to the Minitek and Trio-Tube configurations, the efficiency rate of species identification increased to more than 95% [1].
  • The performance of the sucrose-supplemented Minitek and Trio-Tube systems, compared to the combined results of Micro-ID and aminolevulinic acid, produced correlations of 94 and 90%, respectively [1].
  • METHODS: The 3-tesla MR imaging unit (Siemens Trio) was analyzed and compared with a 1-tesla unit (Siemens Magnetom Expert) and to a 1.5-tesla unit (Philips Gyroscan) [16].
 

Physical interactions of TRIO

  • The RhoA-binding site was mapped to the Trio immunoglobulin-like domain [17].
 

Regulatory relationships of TRIO

  • Herein we provide evidence that Trio not only activates RhoA but is also a RhoA target [17].
 

Other interactions of TRIO

  • Our results indicate that filamin, as a molecular target of Trio, may be a scaffold for the spatial organization of Rho-GTPase-mediated signalling pathways [6].
  • Kalirin isoforms are predominantly expressed in the brain, while Trio is expressed in a wider variety of tissues [18].
 

Analytical, diagnostic and therapeutic context of TRIO

  • Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio [19].
  • MRI contrast enhancement of both agents was studied in nude mice bearing MDA-BM-231 human breast carcinoma xenografts, on a Siemens Trio 3T scanner [20].
  • Enantiomeric separation and quantification of pindolol in human plasma by chiral liquid chromatography/tandem mass spectrometry using staggered injection with a CTC Trio Valve system [21].
  • The present work was undertaken to study the comparative rheology of three tooth bleaching systems: two gels (Opalescence, Ultradent; Perfecta Trio, American Dental Hygienics) and a paste (Colgate Platinum, Colgate) [22].

References

  1. Rapid species identification and biotyping of respiratory isolates of Haemophilus spp. Matthews, J.S., Reynolds, J.A., Weesner, D.E., Perry, J.L., Jenkins, A.L. J. Clin. Microbiol. (1983) [Pubmed]
  2. Evaluation of a new dipslide with a selective medium for the rapid detection of beta-glucuronidase-positive Escherichia coli. Larinkari, U., Rautio, M. Eur. J. Clin. Microbiol. Infect. Dis. (1995) [Pubmed]
  3. Uricult trio as a screening test for bacteriuria in pregnancy. Greeff, A., Jeffery, B., Pattinson, R.C. S. Afr. Med. J. (2002) [Pubmed]
  4. Comparison of intracranial 3D-ToF-MRA with and without parallel acquisition techniques at 1.5T and 3.0T: preliminary results. Gaa, J., Weidauer, S., Requardt, M., Kiefer, B., Lanfermann, H., Zanella, F.E. Acta radiologica (Stockholm, Sweden : 1987) (2004) [Pubmed]
  5. NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. Liu, X., Wang, H., Eberstadt, M., Schnuchel, A., Olejniczak, E.T., Meadows, R.P., Schkeryantz, J.M., Janowick, D.A., Harlan, J.E., Harris, E.A., Staunton, D.E., Fesik, S.W. Cell (1998) [Pubmed]
  6. The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin. Bellanger, J.M., Astier, C., Sardet, C., Ohta, Y., Stossel, T.P., Debant, A. Nat. Cell Biol. (2000) [Pubmed]
  7. 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. Debant, A., Serra-Pagès, C., Seipel, K., O'Brien, S., Tang, M., Park, S.H., Streuli, M. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Assignment of TRIO, the Trio gene (PTPRF interacting) to human chromosome bands 5p 15.1-->p 14 by in situ hybridization. Taviaux, S., Diriong, S., Bellanger, J.M., Streuli, M., Debant, A. Cytogenet. Cell Genet. (1997) [Pubmed]
  9. The Human Rho-GEF trio and its target GTPase RhoG are involved in the NGF pathway, leading to neurite outgrowth. Estrach, S., Schmidt, S., Diriong, S., Penna, A., Blangy, A., Fort, P., Debant, A. Curr. Biol. (2002) [Pubmed]
  10. An alternative transcript derived from the trio locus encodes a guanosine nucleotide exchange factor with mouse cell-transforming potential. Yoshizuka, N., Moriuchi, R., Mori, T., Yamada, K., Hasegawa, S., Maeda, T., Shimada, T., Yamada, Y., Kamihira, S., Tomonaga, M., Katamine, S. J. Biol. Chem. (2004) [Pubmed]
  11. Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization. Seipel, K., O'Brien, S.P., Iannotti, E., Medley, Q.G., Streuli, M. J. Cell. Sci. (2001) [Pubmed]
  12. Mechanisms of guanine nucleotide exchange and Rac-mediated signaling revealed by a dominant negative trio mutant. Debreceni, B., Gao, Y., Guo, F., Zhu, K., Jia, B., Zheng, Y. J. Biol. Chem. (2004) [Pubmed]
  13. Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth. Seipel, K., Medley, Q.G., Kedersha, N.L., Zhang, X.A., O'Brien, S.P., Serra-Pages, C., Hemler, M.E., Streuli, M. J. Cell. Sci. (1999) [Pubmed]
  14. Solo/Trio8, a membrane-associated short isoform of Trio, modulates endosome dynamics and neurite elongation. Sun, Y.J., Nishikawa, K., Yuda, H., Wang, Y.L., Osaka, H., Fukazawa, N., Naito, A., Kudo, Y., Wada, K., Aoki, S. Mol. Cell. Biol. (2006) [Pubmed]
  15. The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids. Skowronek, K.R., Guo, F., Zheng, Y., Nassar, N. J. Biol. Chem. (2004) [Pubmed]
  16. Analyzing 3-tesla magnetic resonance imaging units for implementation in radiosurgery. Mack, A., Wolff, R., Scheib, S., Rieker, M., Weltz, D., Mack, G., Kreiner, H.J., Pilatus, U., Zanella, F.E., Böttcher, H.D., Seifert, V. J. Neurosurg. (2005) [Pubmed]
  17. The trio guanine nucleotide exchange factor is a RhoA target. Binding of RhoA to the trio immunoglobulin-like domain. Medley, Q.G., Serra-Pagès, C., Iannotti, E., Seipel, K., Tang, M., O'Brien, S.P., Streuli, M. J. Biol. Chem. (2000) [Pubmed]
  18. Genomic organization and differential expression of Kalirin isoforms. McPherson, C.E., Eipper, B.A., Mains, R.E. Gene (2002) [Pubmed]
  19. Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio. Skowronek, K., Ghumman, M., Zheng, Y., Nassar, N. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  20. Contrast-enhanced MRI with new biodegradable macromolecular Gd(III) complexes in tumor-bearing mice. Zong, Y., Wang, X., Goodrich, K.C., Mohs, A.M., Parker, D.L., Lu, Z.R. Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. (2005) [Pubmed]
  21. Enantiomeric separation and quantification of pindolol in human plasma by chiral liquid chromatography/tandem mass spectrometry using staggered injection with a CTC Trio Valve system. Wang, H., Shen, Z. Rapid Commun. Mass Spectrom. (2006) [Pubmed]
  22. Rheological characteristics of tooth bleaching materials. Wille, T., Combe, E.C., Pesun, I.J., Giles, D.W. Journal of oral rehabilitation. (2000) [Pubmed]
 
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