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Disposing of misfolded ER proteins: A troubled substrate's way out of the ER.

Abstract：

:Secreted, plasma membrane, and resident proteins of the secretory pathway are synthesized in the endoplasmic reticulum (ER) where they undergo post-translational modifications, oxidative folding, and subunit assembly in tightly monitored processes. An ER quality control (ERQC) system oversees protein maturation and ensures that only those reaching their native state will continue trafficking into the secretory pathway to reach their final destinations. Those that fail must be recognized and eliminated to maintain ER homeostasis. Two cellular mechanisms have been identified to rid the ER of terminally unfolded, misfolded, and aggregated proteins. ER-associated degradation (ERAD) was discovered nearly 30 years ago and entails the identification of improperly matured secretory pathway proteins and their retrotranslocation to the cytosol for degradation by the ubiquitin-proteasome system. ER-phagy has been more recently described and caters to larger, more complex proteins and protein aggregates that are not readily handled by ERAD. This pathway has unique upstream components and relies on the same downstream effectors of autophagy used in other cellular processes to deliver clients to lysosomes for degradation. In this review, we describe the main elements of ERQC, ERAD, and ER-phagy and focus on recent advances in these fields.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

Oikonomou C,Hendershot LM

doi

10.1016/j.mce.2019.110630

subject

Has Abstract

pub_date

2020-01-15 00:00:00

pages

110630

eissn

0303-7207

issn

1872-8057

pii

S0303-7207(19)30332-6

journal_volume

500

pub_type

杂志文章,评审

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