Abstract
Coat protein complex II (COPII) plays an essential role in the export of cargo molecules such as secretory proteins, membrane proteins, and lipids from the endoplasmic reticulum (ER). In yeast, the COPII machinery is critical for cell viability as most COPII knockout mutants fail to survive. In mice and fish, homozygous knockout mutants of most COPII genes are embryonic lethal, reflecting the essentiality of the COPII machinery in the early stages of vertebrate development. In humans, COPII mutations, which are often hypomorphic, cause diseases having distinct clinical features. This is interesting as the fundamental cellular defect of these diseases, that is, failure of ER export, is similar. Analyses of humans and animals carrying COPII mutations have revealed clues to why a similar ER export defect can cause such different diseases. Previous reviews have focused mainly on the deficit of secretory or membrane proteins in the final destinations because of an ER export block. In this review, we also underscore the other consequence of the ER export block, namely ER stress triggered by the accumulation of cargo proteins in the ER.
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The authors thank Leah Wabel for proofreading the manuscript. This work was supported by the National Institute of General Medical Sciences of the National Institutes of Health under award number R01GM110373 to J.K.
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Lu, CL., Kim, J. Consequences of mutations in the genes of the ER export machinery COPII in vertebrates. Cell Stress and Chaperones 25, 199–209 (2020). https://doi.org/10.1007/s12192-019-01062-3
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DOI: https://doi.org/10.1007/s12192-019-01062-3