GSK-3 Phosphorylates δ-Catenin and Negatively Regulates Its Stability via Ubiquitination/Proteosome-mediated Proteolysis

δ-Catenin was first identified because of its interaction with presenilin-1, and its aberrant expression has been reported in various human tumors and in patients with Cri-du-Chat syndrome, a form of mental retardation. However, the mechanism whereby δ-catenin is regulated in cells has not been full...

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Veröffentlicht in:	The Journal of biological chemistry 2009-10, Vol.284 (42), p.28579-28589
Hauptverfasser:	Oh, Minsoo, Kim, Hangun, Yang, Ilhwan, Park, Ja-Hye, Cong, Wei-Tao, Baek, Moon-Chang, Bareiss, Sonja, Ki, Hyunkyoung, Lu, Qun, No, Jinhyung, Kwon, Inho, Choi, Jung-Kap, Kim, Kwonseop
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Catenins Cell Adhesion Molecules - metabolism Culture Media, Conditioned - pharmacology Enzyme Inhibitors - pharmacology Fibroblasts - metabolism Glycogen Synthase Kinase 3 - metabolism Glycogen Synthase Kinase 3 beta Humans Mice Neurons - metabolism Phosphoproteins - metabolism Phosphorylation Proteasome Endopeptidase Complex - chemistry Protein Synthesis, Post-Translational Modification, and Degradation Rats Rats, Sprague-Dawley Ubiquitin - chemistry
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