Orchestration of secretory protein folding by ER chaperones.

Orchestration of secretory protein folding by ER chaperones.
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DOI:
10.1016/j.bbamcr.2013.03.007
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发表时间:
2013-11
影响因子:
5.1
通讯作者:
Argon, Yair
Argon, Yair
中科院分区:
生物学2区
文献类型:
--
作者:
Gidalevitz, Tali;Stevens, Fred;Argon, Yair

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The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The secretome has distinct structural and post-translational characteristics, since folding in the ER occurs in an environment that is distinct in terms of its ionic composition, dynamics and requirements for quality contol. The folding machinery in the ER therefore includes chaperones and folding enzymes that introduce, monitor and react to disulfide bonds, glycans, and fluctuations of luminal calcium. We describe the major chaperone networks in the lumen and discuss how they have distinct modes of operation that enable cells to accomplish highly efficient production of the secretome.
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