PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26251180-10 2015 This work identifies FAK as a target of p110delta PI3K that links RhoA with PTEN and establishes for the first time that PTEN is a substrate of FAK-mediated Tyr phosphorylation. Tyrosine 157-160 ras homolog family member A Mus musculus 66-70 24398689-6 2014 Mass spectroscopy identified a single nitration site, located at Tyr(34) in RhoA. Tyrosine 65-68 ras homolog family member A Mus musculus 76-80 24398689-11 2014 Molecular dynamics simulations suggested that the mechanism by which Tyr(34) nitration stimulates RhoA activity was through a decrease in GDP binding to the protein caused by a conformational change within a region of Switch I, mimicking the conformational shift observed when RhoA is bound to a guanine nucleotide exchange factor. Tyrosine 69-72 ras homolog family member A Mus musculus 98-102 24398689-11 2014 Molecular dynamics simulations suggested that the mechanism by which Tyr(34) nitration stimulates RhoA activity was through a decrease in GDP binding to the protein caused by a conformational change within a region of Switch I, mimicking the conformational shift observed when RhoA is bound to a guanine nucleotide exchange factor. Tyrosine 69-72 ras homolog family member A Mus musculus 277-281 15848799-5 2005 Tyrosine phosphorylation of ephexin1 enhances ephexin1"s GEF activity toward RhoA while not altering its activity toward Rac1 or Cdc42, thus changing the balance of GTPase activities. Tyrosine 0-8 ras homolog family member A Mus musculus 77-81 23027962-7 2012 We demonstrate that RhoA, one of the proteins associated with actin, can be phosphorylated on two tyrosine residues within the switch regions, suggesting that phosphorylation of these residues might modulate RhoA signaling to the actin cytoskeleton. Tyrosine 98-106 ras homolog family member A Mus musculus 20-24 23027962-7 2012 We demonstrate that RhoA, one of the proteins associated with actin, can be phosphorylated on two tyrosine residues within the switch regions, suggesting that phosphorylation of these residues might modulate RhoA signaling to the actin cytoskeleton. Tyrosine 98-106 ras homolog family member A Mus musculus 208-212 19361585-4 2009 We found previously that RhoA is expressed in osteoblastic cells and is translocated to the plasma membrane and activated by PTH 1-34 as well as by Nleu(8,18) Tyr(34) PTH 3-34 amide, a PTH analog that does not increase cAMP. Tyrosine 159-162 ras homolog family member A Mus musculus 25-29 18195107-7 2008 p190RhoGEF overexpression enhances RhoA activation and FA formation in MEFs dependent on FAK binding and associated with p190RhoGEF FA recruitment and tyrosine phosphorylation. Tyrosine 151-159 ras homolog family member A Mus musculus 35-39 15705584-3 2005 We also found that although active RhoA, Rac1, and Cdc42 could all mediate Ser-727 and Tyr-705 phosphorylation and nuclear translocation of STAT3, the Rho GTPases were able to induce STAT3 activation independently of the interleukin-6 autocrine pathway, and active RhoA, Rac1, or Cdc42 could not form a stable complex with STAT3 as previously suggested, indicating an unappreciated mechanism of STAT3 activation by the Rho GTPases. Tyrosine 87-90 ras homolog family member A Mus musculus 35-39 18182571-4 2008 Using model REN cells expressing a series of PECAM-1 deletion and point mutants, we found that the PECAM-1 cytoplasmic domain and, more precisely, PECAM-1 tyrosine 686, is critical in mediating RhoA activation and recruitment of EGFP-RhoA to anti-PECAM/NC binding sites at the plasmalemma, actin polymerization into phalloidin-positive stress fibers, and finally CAM endocytosis of anti-PECAM/NCs. Tyrosine 155-163 ras homolog family member A Mus musculus 194-198 18182571-4 2008 Using model REN cells expressing a series of PECAM-1 deletion and point mutants, we found that the PECAM-1 cytoplasmic domain and, more precisely, PECAM-1 tyrosine 686, is critical in mediating RhoA activation and recruitment of EGFP-RhoA to anti-PECAM/NC binding sites at the plasmalemma, actin polymerization into phalloidin-positive stress fibers, and finally CAM endocytosis of anti-PECAM/NCs. Tyrosine 155-163 ras homolog family member A Mus musculus 234-238 7527052-0 1994 The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions. Tyrosine 95-103 ras homolog family member A Mus musculus 4-8 7527052-11 1994 The results suggest that both pp125FAK and paxillin undergo changes in tyrosine phosphorylation upon activation of rhoA, and that these changes are associated with the assembly of focal adhesions and actin stress fibres. Tyrosine 71-79 ras homolog family member A Mus musculus 115-119 33248422-6 2021 We have shown that the activation of RhoA in lipopolysaccharide (LPS)-mediated ALI, is dependent, at least in part, on a single nitration event at tyrosine (Y)34. Tyrosine 147-155 ras homolog family member A Mus musculus 37-41 30568170-3 2019 We discovered that treatment of CLL cells with Wnt5a causes Receptor tyosin kinase-like orphan receptor 1 (ROR1) to bind cortactin, which undergoes tyrosine phosphorylation at Y421, recruits ARHGEF1, and activates RhoA, thereby enhancing leukemia-cell migration; such effects could be inhibited by cirmtuzumab, a humanized mAb specific for ROR1. Tyrosine 148-156 ras homolog family member A Mus musculus 214-218 31667337-3 2019 Wnt5a also induced ROR1-dependent tyrosine phosphorylation of cortactin (Y421), which recruited ARHGEF1 to activate RhoA and promote breast-cancer-cell migration; such effects could be inhibited by cirmtuzumab, a humanized mAb specific for ROR1. Tyrosine 34-42 ras homolog family member A Mus musculus 116-120 28316141-11 2017 These results suggest that the inhibition of tyrosine phosphorylation of the focal adhesion plaque components by dasatinib may alter the assembly of actin fibers resulting in the activation of RhoA/ROCK pathway. Tyrosine 45-53 ras homolog family member A Mus musculus 193-197