期刊
NATURE CELL BIOLOGY
卷 14, 期 1, 页码 93-U176出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2383
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资金
- NIH
- Ludwig Institute for Cancer Research
- NRSA from NIH
- Damon Runyon Cancer Research Foundation [DRG 1974-08]
Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have beenidentified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD.
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