IndraLab

Statements

SRC phosphorylates TIAM1 on Y384. 9 / 10
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rlimsp
"Here, we show that Tiam1 is phosphorylated on Y384 by Src."
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reach
"We found that Tiam1 constitutively forms a complex with ERK, and this Tiam1 associated ERK is only activated when Tiam1 is phosphorylated on Y384 by Src."
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sparser
"To establish whether endogenous Src family kinases (SFKs) phosphorylate endogenous Tiam1 on Y384, we treated H293T cells with sodium pervanadate (PV), an irreversible protein-tyrosine phosphatase inhi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Here, we show that Tiam1 is phosphorylated on Y384 by Src."
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sparser
"This interaction required both the typical binding pocket of the Grb2 SH2 domain ( Figure S5 A) and Src-induced phosphorylation of Tiam1 on Y384 ( Figure 4 B)."
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sparser
"We found that Tiam1 constitutively forms a complex with ERK, and this Tiam1-associated ERK is only activated when Tiam1 is phosphorylated on Y384 by Src."
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reach
"To establish whether endogenous Src family kinases (SFKs) phosphorylate endogenous Tiam1 on Y384, we treated H293T cells with sodium pervanadate (PV), an irreversible protein-tyrosine phosphatase inhi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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reach
"Together, these data support our previous findings that phosphorylation of Tiam1 at Y384 is induced by Src activity and is associated with reduced total Tiam1 levels.Here, we have shown that Tiam1 is [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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reach
"Here, we show that Tiam1 is phosphorylated on Y384 by Src."
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SRC phosphorylates TIAM1. 9 / 9
1 | 3 5
reach
"Src dependent phosphorylation of Tiam1 has been recently implicated in the Rac activation induced by another barrier-protective agonist, sphingosine 1-phosphate (Gonzalez et al., 2006)."
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signor
"Tiam1 cooperated with src to induce activation of rac1 in vivo and the formation of membrane ruffles."
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sparser
"Rac1 activity may be regulated by Src-dependent tyrosine phosphorylation of Vav2 and Tiam1 [148] ."
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reach
"Src, which is also activated in focal adhesions XREF_BIBR, XREF_BIBR, can phosphorylate p130Cas, which phosphorylates and activates the Rac1 GEF DOCK180 XREF_BIBR, XREF_BIBR, or can directly phosphorylate and activate the Rac1 GEFs Vav and Tiam1 XREF_BIBR, XREF_BIBR."
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sparser
"Src-dependent phosphorylation of Tiam1 has been recently implicated in the Rac activation induced by another barrier-protective agonist, sphingosine 1-phosphate ( Gonzalez et al., 2006 )."
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reach
"In support of our data, it was reported that active c-Src can phosphorylate and potentiate Tiam1, a guanine nucleotide exchange factor (GEF) which exhibits the highest specificity for Rac1, indicating that Rac1 is mainly activated by c-Src via Tiam1 XREF_BIBR."
27881869
sparser
"Thus, these data reveal that, at initial stages of EMT, the fraction of Tiam1 associated with AJs is preferentially depleted (relative to cytoplasmic Tiam1) as a consequence of Src-induced Tiam1 phosp[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Research has found that the tyrosine phosphorylation of β catenin and Tiam 1 by Src suppresses the association of β catenin with E-cadherin and disrupts the integrity of cell-to-cell junctions [ xref ]."
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sparser
"Tyrosine phosphorylation of β catenin and Tiam 1 by Src and Src/FAK complex suppresses the association of β catenin with E-cadherin and disrupts the integrity of adherens junctions, a critical step in epithelial to mesenchymal transition [ xref – xref ]."
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SRC phosphorylated on Y419 phosphorylates TIAM1 on Y384. 1 / 1
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biopax:pid
No evidence text available
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SRC phosphorylates TIAM1 on tyrosine. 1 / 1
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reach
"Rac1 activity may be regulated by Src dependent tyrosine phosphorylation of Vav2 and Tiam1 [148]."
29330095
Kinase-active SRC phosphorylates TIAM1 on tyrosine. 1 / 1
1 |
bel
"We further show that Vav2 and the ubiquitously expressed Rac1 guanine nucleotide exchange factor Tiam1 are phosphorylated in tyrosine residues in cells transfected with active and oncogenic Src.Moreover, phosphorylation of Tiam1 in cells treated with pervanadate, a potent inhibitor of tyrosine phosphatases, was partially inhibited by the Src inhibitor SU6656."
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