| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.68040663 |
| Using the interaction trap assay to identify candidate proteins that bind the cytoplasmic region of the LAR transmembrane protein tyrosine phosphatase ( PT Pase ) , we isolated a cDNA encoding a 2861 amino acid protein termed Trio that contains three enzyme domains : two functional GEF domains and a protein serine / threonine kinase ( PSK ) domain . 0.68040663^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| Assignment of TRIO , the Trio gene ( PTPRF interacting ) to human chromosome bands 5p 15 . 1 > p 14 by in situ hybridization . ^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| Recent reports indicate that this role involves interaction with several different protein families , including LAR phosphatases , catenin / cadherin cell adhesion complexes , Trio family GEFs , and Ena / VASP family actin regulatory proteins . ^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| Here , we describe the identification and characterization of the Drosophila counterpart of Trio , a guanine nucleotide exchange factor ( GEF ) that associates with the receptor phosphatase LAR and regulates GTPase activation in vertebrate cells . ^^^ Moreover , reduction of trio activity potentiates the phenotype of mutations in the LAR homolog Dlar , suggesting that these proteins collaborate in orchestrating the cytoskeletal events that underlie normal axonogenesis . . ^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| Trio was originally identified as a LAR tyrosine phosphatase binding protein and is involved in actin remodeling , cell migration , and cell growth . ^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| Genetic interactions implicate both Enabled and Trio in LAR signal transduction . . ^^^ |
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| Interacting proteins: O75962 and P10586 |
Pubmed |
SVM Score :0.0 |
| The association of Trio with the Lar tyrosine phosphatase led us to study the role of tyrosine phosphorylation in Trio function using focal adhesion kinase ( FAK ) . ^^^ The Lar interacting domain of Trio is constitutively tyrosine phosphorylated when expressed in COS 7 cells and was highly phosphorylated when it was co transfected with FAK . ^^^ |
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