The cochaperone BAG3 coordinates protein synthesis and autophagy under mechanical strain through spatial regulation of mTORC1

详细信息    查看全文

• 作者：Barbara Kathage^a ; Sebastian Gehlert^b ; Anna Ulbricht^a ; Laura Lü ; decke^a ; Victor E. Tapia^c ; Zacharias Orfanos^a ; Daniela Wenzel^d ; Wilhelm Bloch^b ; Rudolf Volkmer^c ; Bernd K. Fleischmann^d ; Dieter O. Fü ; rst^a ; & Jö ; rg Hö ; hfeld^a ; ^{hoehfeld@uni-bonn.de}
• 关键词：BAG3 ; BCL2-associated athanogene ; mTOR ; mammalian target of rapamycin ; mTORC1 ; mammalian target of rapamycin complex 1 ; TSC ; tuberous sclerosis ; CASA ; chaperone-assisted selective autophagy ; CMA ; chaperone-mediated autophagy ; RE ; maximal eccentric resistance exercise ; ES ; electrical stimulation ; MBP ; maltose-binding protein ; CBD ; chitin-binding domain
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1864
• 期：1
• 页码：62-75
• 全文大小：3667 K
• 卷排序：1864

文摘

The cochaperone BAG3 interacts with the mTOR inhibitor TSC1. BAG3 recruits TSC complexes and mTOR vesicles to the actin cytoskeleton. mTORC1 inhibition is essential for BAG3-mediated autophagy at the cytoskeleton. BAG3 activates mTORC1 throughout the cytoplasm and stimulates protein synthesis.