title: mTORC2 phosphorylates protein kinase Cζ to regulate its stability and activity.
abstract: Protein kinase Cζ (PKCζ) is phosphorylated at the activation loop and the turn motif (TM). However, the TM kinase and functional relevance of TM phosphorylation remain largely unknown. We demonstrate that PKCζ TM is phosphorylated directly by the mTORC2 complex, and this phosphorylation is required for maintaining PKCζ kinase activity and stability. Functionally, mTORC2 regulates the activity of Rho family of GTPases, and therefore the organization of the actin cytoskeleton, through the control of PKCζ activity. Taken together, our findings identify PKCζ as a novel substrate and downstream effector of mTORC2 signaling.
authors.affiliation: Markey Cancer Center, University of Kentucky, Lexington, KY, USA.
authors.forename: Xin
authors.initials: X
authors.lastname: Li
authors.forename: Tianyan
authors.initials: T
authors.lastname: Gao
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D002460:Cell Line; D004795:Enzyme Stability; D057809:HEK293 Cells; D006801:Humans; D000076225:Mechanistic Target of Rapamycin Complex 2; D051379:Mice; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D000099221:Protein Kinase C zeta
chemical_list: D000076225:Mechanistic Target of Rapamycin Complex 2; D046912:Multiprotein Complexes; D011493:Protein Kinase C; D058570:TOR Serine-Threonine Kinases; D000099221:Protein Kinase C zeta