Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is mediated by CUL7 E3 ligase

Expression of the hominoid-specific TBC1D3 oncoprotein enhances growth factor receptor signaling and subsequently promotes cellular proliferation and survival. Here we report that TBC1D3 is degraded in response to growth factor signaling, suggesting that TBC1D3 expression is regulated by a growth fa...

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Veröffentlicht in:	PloS one 2012-09, Vol.7 (9), p.e46485-e46485
Hauptverfasser:	Kong, Chen, Samovski, Dmitri, Srikanth, Priya, Wainszelbaum, Marisa J, Charron, Audra J, Liu, Jialiu, Lange, Jeffrey J, Chen, Pin-I, Pan, Zhen-Qiang, Su, Xiong, Stahl, Philip D
Format:	Artikel
Sprache:	eng
Schlagworte:	Adapter proteins Alkaline phosphatase Biodegradation Biology Cancer Care and treatment Cell growth Cell survival Chromosomes Cullin Proteins - metabolism Degradation Epidermal growth factor F-Box Proteins - metabolism Feedback loops Genomes Growth factor receptors GTPase-Activating Proteins - metabolism HeLa Cells Humans Insulin Intercellular Signaling Peptides and Proteins - physiology Kinases Leupeptins - pharmacology Ligases Medical screening Medicine Negative feedback Oncoproteins Phosphorylation Physiology Post-translation Proteasome Inhibitors - pharmacology Protein Binding Protein Processing, Post-Translational Proteolysis Proto-Oncogene Proteins - metabolism Regulation Scaffolding Signaling Tumors Two-Hybrid System Techniques Ubiquitin Ubiquitin-protein ligase Ubiquitin-Protein Ligases - metabolism Ubiquitination Yeast
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