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Full-Text Articles in Physiology
The Identification Of Novel Protein-Protein Interactions In Liver That Affect Glucagon Receptor Activity, Junfeng Han, Ming Zhang, Sean Froese, Feihan F. Dai, Mélanie Robitaille, Alpana Bhattacharjee, Xinyu Huang, Weiping Jia, Stéphane Angers, Michael B. Wheeler, Li Wei
The Identification Of Novel Protein-Protein Interactions In Liver That Affect Glucagon Receptor Activity, Junfeng Han, Ming Zhang, Sean Froese, Feihan F. Dai, Mélanie Robitaille, Alpana Bhattacharjee, Xinyu Huang, Weiping Jia, Stéphane Angers, Michael B. Wheeler, Li Wei
Faculty Publications
Glucagon regulates glucose homeostasis by controlling glycogenolysis and gluconeogenesis in the liver. Exaggerated and dysregulated glucagon secretion can exacerbate hyperglycemia contributing to type 2 diabetes (T2D). Thus, it is important to understand how glucagon receptor (GCGR) activity and signaling is controlled in hepatocytes. To better understand this, we sought to identify proteins that interact with the GCGR to affect ligand-dependent receptor activation. A Flag-tagged human GCGR was recombinantly expressed in Chinese hamster ovary (CHO) cells, and GCGR complexes were isolated by affinity purification (AP). Complexes were then analyzed by mass spectrometry (MS), and protein-GCGR interactions were validated by co-immunoprecipitation (Co-IP) …
Distinct Phospho-Forms Of Cortactin Differentially Regulate Actin Polymerization And Focal Adhesions, Anne E. Kruchten, Eugene W. Krueger, Yu Wang, Mark A. Mcniven
Distinct Phospho-Forms Of Cortactin Differentially Regulate Actin Polymerization And Focal Adhesions, Anne E. Kruchten, Eugene W. Krueger, Yu Wang, Mark A. Mcniven
Faculty Publications
Cortactin is an actin-binding protein that is overexpressed in many cancers and is a substrate for both tyrosine and serine/threonine kinases. Tyrosine phosphorylation of cortactin has been observed to increase cell motility and invasion in vivo, although it has been reported to have both positive and negative effects on actin polymerization in vitro. In contrast, serine phosphorylation of cortactin has been shown to stimulate actin assembly in vitro. Currently, the effects of cortactin serine phosphorylation on cell migration are unclear, and furthermore, how the distinct phospho-forms of cortactin may differentially contribute to cell migration has not been directly compared. Therefore, …