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Trends Cell Biol. 2017 Jun;27(6):430-440. doi: 10.1016/j.tcb.2016.12.002. Epub 2017 Feb 9.

New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation.

Author information

1
Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48105, USA; Division of Metabolism, Endocrinology and Diabetes, University of Michigan Medical School, Ann Arbor, MI 48105, USA. Electronic address: lingq@med.umich.edu.
2
Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48105, USA.
3
Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48105, USA; Division of Metabolism, Endocrinology and Diabetes, University of Michigan Medical School, Ann Arbor, MI 48105, USA.

Abstract

Many human diseases are associated with mutations causing protein misfolding and aggregation in the endoplasmic reticulum (ER). ER-associated degradation (ERAD) is a principal quality-control mechanism responsible for targeting misfolded ER proteins for cytosolic degradation. However, despite years of effort, the physiological role of ERAD in vivo remains largely unknown. Several recent studies have reported intriguing phenotypes of mice deficient for ERAD function in specific cell types. These studies highlight that mammalian ERAD has been designed to perform a wide-range of cell-type-specific functions in vivo in a substrate-dependent manner.

PMID:
28131647
PMCID:
PMC5440201
DOI:
10.1016/j.tcb.2016.12.002
[Indexed for MEDLINE]
Free PMC Article

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