TRIO (gene)

TRIO

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1NTY, 2NZ8

Identifiers

Aliases

TRIO, ARHGEF23, tgat, trio Rho guanine nucleotide exchange factor

External IDs

MGI: 1927230 HomoloGene: 20847 GeneCards: TRIO

Genetically Related Diseases

neuropathy^[1]

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 • enzyme 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 • positive regulation of GTPase activity
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


7204


223435

Ensembl


ENSG00000038382


ENSMUSG00000022263

UniProt


O75962


Q0KL02

RefSeq (mRNA)


NM_007118


NM_001081302

RefSeq (protein)


NP_009049.2


NP_001074771.1

Location (UCSC)

Chr 5: 14.14 – 14.53 Mb

Chr 15: 27.73 – 28.03 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.^[4]^[5]

Interactions

TRIO (gene) has been shown to interact with Filamin^[6] and RHOA.^[7]

References

↑ "Diseases that are genetically associated with TRIO view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.

PDB gallery

1nty: Crystal structure of the first DH/PH domain of Trio to 1.7 A

2nz8: N-terminal DHPH cassette of Trio in complex with nucleotide-free Rac1

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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TRIO (gene)

Interactions

References

Further reading