Tipping the Delicate Balance: Defining How Proteasome Maturation Affects the Degradation of
a Substrate for Autophagy and Endoplasmic
柯基断尾Reticulum Associated Degradation (ERAD)
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白醋去水垢期刊名称： Autophagy
作者： Brodsky, Jeffrey L., Scott, Craig M.经典老歌有哪些
年份： 2007年
四川过年习俗期号： 第6期
酒虫关键词： anti-trypsin;A1Pi;proteasome;chaperone;proteasome asmbly常用的修辞手法
chaperone;PAC;yeast;unfolded protein respon;liver dia;apoptosis
摘要：An increasing body of data links endoplasmic reticulum (ER) function to autophagy. Not surpri
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singly, then, some aberrant proteins in the ER can be destroyed either via ER associated degradation (ERAD), which is proteasome-mediated, or via autophagy. One such substrate is the Z variant of the alpha-1 protea inhibitor (A1Pi), variably known as A1Pi-Z or AT-Z (anti-trypsin, Z variant). The wild type protein is primarily synthesized in the liver and is creted. In contrast, AT-Zlike other ERAD substratesis retro-translocated from the ER and delivered to the proteasome. However, AT-Z can form high molecular weight polymers that are degraded via autophagy, and cells that accumulate AT-Z polymers ultimately succumb, which leads to liver dia. Therefore, identifying genes that have an impact AT-Z turnover reprents an active
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