Title : Receptor tyrosine kinase activation of RhoA is mediated by AKT phosphorylation of DLC1.

Pub. Date : 2017 Dec 4

PMID : 29114068






7 Functional Relationships(s)
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1 We report several receptor tyrosine kinase (RTK) ligands increase RhoA-guanosine triphosphate (GTP) in untransformed and transformed cell lines and determine this phenomenon depends on the RTKs activating the AKT serine/threonine kinase. Guanosine Triphosphate ras homolog family member A Homo sapiens
2 We report several receptor tyrosine kinase (RTK) ligands increase RhoA-guanosine triphosphate (GTP) in untransformed and transformed cell lines and determine this phenomenon depends on the RTKs activating the AKT serine/threonine kinase. Guanosine Triphosphate ras homolog family member A Homo sapiens
3 The increased RhoA-GTP results from AKT phosphorylating three serines (S298, S329, and S567) in the DLC1 tumor suppressor, a Rho GTPase-activating protein (RhoGAP) associated with focal adhesions. Guanosine Triphosphate ras homolog family member A Homo sapiens
4 That binding, which interferes with the interaction of RhoA-GTP with the RhoGAP domain, reduces the hydrolysis of RhoA-GTP, the binding of other DLC1 ligands, and the colocalization of DLC1 with focal adhesions and attenuates tumor suppressor activity. Guanosine Triphosphate ras homolog family member A Homo sapiens
5 That binding, which interferes with the interaction of RhoA-GTP with the RhoGAP domain, reduces the hydrolysis of RhoA-GTP, the binding of other DLC1 ligands, and the colocalization of DLC1 with focal adhesions and attenuates tumor suppressor activity. Guanosine Triphosphate ras homolog family member A Homo sapiens
6 That binding, which interferes with the interaction of RhoA-GTP with the RhoGAP domain, reduces the hydrolysis of RhoA-GTP, the binding of other DLC1 ligands, and the colocalization of DLC1 with focal adhesions and attenuates tumor suppressor activity. Guanosine Triphosphate ras homolog family member A Homo sapiens
7 That binding, which interferes with the interaction of RhoA-GTP with the RhoGAP domain, reduces the hydrolysis of RhoA-GTP, the binding of other DLC1 ligands, and the colocalization of DLC1 with focal adhesions and attenuates tumor suppressor activity. Guanosine Triphosphate ras homolog family member A Homo sapiens