Abstract
Following translocation into the rough endoplasmic reticulum (ER), secretory proteins undergo a series of folding, maturation, compartmentalization and trafficking events. These are finely tuned to avoid misfolded protein accumulation and the consequent ER stress. Misfolded proteins and components of the ER quality control and ER-associated degradation (ERAD) machineries concentrate in mammalian cells in the pericentriolar ER-derived quality control compartment (ERQC), a staging ground for ERAD. We have recently determined that, surprisingly, trafficking to the ERQC and delivery to ERAD are dependent on COPII-coated vesicle transport and that they can be retrieved to the peripheral ER in COPI-coated vesicles.
Funding
This research was funded by Israel Science Foundation grant numbers 1593/16 and 2577/20.
Institutional Review Board Statement
Not applicable.
Informed Consent Statement
Not applicable.
Data Availability Statement
Data available upon request.
Acknowledgments
I would like to thank members of the Lederkremer lab.
Conflicts of Interest
The author declares no conflict of interest.
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