Modulation of fatty acid synthase degradation by concerted action of p38 MAP kinase, E3 ligase COP1 and SH2-tyrosine phosphatase Shp2
作者： Jianxiu Yu , Rong Deng , Helen H. Zhu , Sharon S. Zhang , Changhong Zhu
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摘要: The Src-homology 2 (SH2) domain-containing tyrosine phosphatase Shp2 has been known to regulate various signaling pathways triggered by receptor and cytoplasmic kinases. Here we describe a novel function of in control lipid metabolism mediating degradation fatty acid synthase (FASN). p38-phosphorylated COP1 accumulates the cytoplasm subsequently binds FASN through here as an adapter, leading FASN-Shp2-COP1 complex formation mediated ubiquitination pathway. By fasting p38 is activated stimulates protein mice. Consistently, levels are dramatically elevated mouse liver pancreas which Shp2/Ptpn11 selectively deleted. Thus, this study identifies new activity for metabolism.
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