| http://purl.uniprot.org/citations/27096001 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27096001 | http://www.w3.org/2000/01/rdf-schema#comment | "The G12 family of heterotrimeric G proteins is defined by their α-subunits, Gα12 and Gα13. These α-subunits regulate cellular homeostasis, cell migration, and oncogenesis in a context-specific manner primarily through their interactions with distinct proteins partners that include diverse effector molecules and scaffold proteins. With a focus on identifying any other novel regulatory protein(s) that can directly interact with Gα13, we subjected Gα13 to tandem affinity purification-coupled mass spectrometric analysis. Our results from such analysis indicate that Gα13 potently interacts with mammalian Ric-8A. Our mass spectrometric analysis data also indicates that Ric-8A, which was tandem affinity purified along with Gα13, is phosphorylated at Ser-436, Thr-441, Thr-443 and Tyr-435. Using a serial deletion approach, we have defined that the C-terminus of Gα13 containing the guanine-ring interaction site is essential and sufficient for its interaction with Ric-8A. Evaluation of Gα13-specific signaling pathways in SKOV3 or HeyA8 ovarian cancer cell lines indicate that Ric-8A potentiates Gα13-mediated activation of RhoA, Cdc42, and the downstream p38MAPK. We also establish that the tyrosine phosphorylation of Ric-8A, thus far unidentified, is potently stimulated by Gα13. Our results also indicate that the stimulation of tyrosine-phosphorylation of Ric-8A by Gα13 is partially sensitive to inhibitors of Src-family of kinases, namely PP2 and SI. Furthermore, we demonstrate that Gα13 promotes the translocation of Ric-8A to plasma membrane and this translocation is attenuated by the Src-inhibitors, SI1 and PP2. Thus, our results demonstrate for the first time that Gα13 stimulates the tyrosine phosphorylation of Ric-8A and Gα13-mediated tyrosine-phosphorylation plays a critical role in the translocation of Ric-8A to plasma membrane."xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.org/dc/terms/identifier | "doi:10.5334/1750-2187-10-3"xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/author | "Yan M."xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/author | "Ha J.H."xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/author | "Dhanasekaran D.N."xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/name | "J Mol Signal"xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/pages | "3"xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/title | "Galpha13 Stimulates the Tyrosine Phosphorylation of Ric-8A."xsd:string |
| http://purl.uniprot.org/citations/27096001 | http://purl.uniprot.org/core/volume | "10"xsd:string |
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