TRAF6-mediated SM22α K21 Ubiquitination Promotes G6PD Activation and NADPH Production, Contributing

来源 :第四届吴宪吴瑞国际学术研讨会、第九届全国医学生物化学与分子生物学、第六届全国临床应用生物化学与分子生物学联合学术讨论会 | 被引量 : 0次 | 上传用户:forisa1
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The pentose phosphate pathway (PPP) plays an essential role in cell proliferation via production of NADPH.Smooth muscle (SM) 22α protein is involved in the regulation of vascular smooth muscle cell (VSMC) phenotypes.Here, we identify the relationship between NADPH production and SM22α activity in the development and progression of vascular diseases.We showed that the expression and activity of Glucose-6-phosphate dehydrogenase (G6PD) is promoted in PDGF-BB-induced proliferative VSMCs.PDGF-BB induced G6PD membrane translocation and activation in a SM22αK21 ubiquitination-dependent manner.The ubiquitinated SM22α interacted with G6PD, and mediated G6PD membrane translocation.Furthermore, we found that TNF receptor associated factor (TRAF) 6 mediated SM22 a K21 ubiquitination in a K63-1inked manner upon PDGF-BB stimulation.Knockdown of TRAF6 decreased the membrane translocation and activity of G6PD, parallel with reduced SM22α K21 ubiquitination.Increased NADPH generation enhanced VSMC viability, and reduced apoptosis in vivo and in vitro via glutathione (GSH) homeostasis.We provide evidence that TRAF6-induced SM22α ubiquitination maintains VSMC survival through increase in G6PD activity and NADPH production.
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