Stabilization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation.
O-Glycosylation modifies and regulates a variety of intracellular proteins. Plakoglobin, which functions in both cell-cell adhesion and signal transduction, is modified by O-glycosylation; however, the significance is unknown. To investigate the functional consequence of plakoglobin O-glycosylation, we cloned and overexpressed in keratinocytes murine O-GlcNAc transferase (mOGT). Over expression of mOGT in murine keratinocytes resulted in (i) glycosylation of plakoglobin and (ii) increased levels of plakoglobin due to post-translational stabilization of plakoglobin. Additionally, overexpression of mOGT in keratinocytes correlated with increased staining for cell-cell adhesion proteins and greater cell-cell adhesion. These observations suggest that O-glycosylation functions to regulate the post-translational stability of plakoglobin and keratinocyte cell-cell adhesion.
Hu
Peiqi
P
Department of Dermatology, University of North Carolina, Chapel Hill, North Carolina 27599-7287, USA.
Berkowitz
Paula
P
Madden
Victoria J
VJ
Rubenstein
David S
DS
D000818:Animals; D002384:Catalysis; D002448:Cell Adhesion; D002460:Cell Line; D003598:Cytoskeletal Proteins / Q000737:chemistry; D003902:Detergents / Q000494:pharmacology; D006031:Glycosylation; D015603:Keratinocytes / Q000378:metabolism*; D051379:Mice; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D051185:gamma Catenin / Q000737:chemistry / Q000502:physiology*
D003598:Cytoskeletal Proteins; D003902:Detergents; D051185:gamma Catenin; D010749:Phosphoprotein Phosphatases