Regulation of membrane trafficking and endocytosis by protein kinase C: emerging role of the pericentrion, a novel protein kinase C-dependent subset of recycling endosomes. Cell Mol Life Sci 2007 Feb;64(3):263-70
Date
12/21/2006Pubmed ID
17180302DOI
10.1007/s00018-006-6363-5Scopus ID
2-s2.0-33846967126 (requires institutional sign-in at Scopus site) 57 CitationsAbstract
The protein kinase C (PKC) family of isoenzymes has been shown to regulate a variety of cellular processes, including receptor desensitization and internalization, and this has sparked interest in further delineation of the roles of specific isoforms of PKC in membrane trafficking and endocytosis. Recent studies have identified a novel translocation of PKC to a juxtanuclear compartment, the pericentrion, which is distinct from the Golgi complex but epicentered on the centrosome. Sustained activation of PKC (longer than 30 min) also results in sequestration of plasma membrane lipids and proteins to the same compartment, demonstrating a global effect on endocytic trafficking. This review summarizes these studies, particularly focusing on the characterization of the pericentrion as a distinct PKC-dependent subset of recycling endosomes. We also discuss emerging insights into a role for PKC as a central hub in regulating vesicular transport pathways throughout the cell, with implications for a wide range of pathobiologic processes, e.g. diabetes and abnormal neurotransmission or receptor desensitization.
Author List
Alvi F, Idkowiak-Baldys J, Baldys A, Raymond JR, Hannun YAAuthor
John R. Raymond MD President, CEO, Professor in the President department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCell Membrane
Endocytosis
Endosomes
Humans
Protein Kinase C
Protein Transport
Signal Transduction