Journal
CELL REPORTS
Volume 28, Issue 10, Pages 2517-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2019.08.006
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Funding
- NIH [R01NS080833, R01AI132387, R01AI139087, R21NS106159, P30DK034854]
- Intelligence Advanced Research Projects Activity (IARPA) [W911NF-17-2-0089]
- National Natural Science Foundation of China [81572255]
- Boston Children's Hospital Intellectual and Developmental Disabilities Research Center [P30HD18655]
- Burroughs Wellcome Fund
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The endoplasmic reticulum (ER) membrane protein complex (EMC) is a key contributor to biogenesis and membrane integration of transmembrane proteins, but our understanding of its mechanisms and the range of EMC-dependent proteins remains incomplete. Here, we carried out an unbiased mass spectrometry (MS)-based quantitative proteomic analysis comparing membrane proteins in EMC-deficient cells to wild-type (WT) cells and identified 36 EMC-dependent membrane proteins and 171 EMC-independent membrane proteins. Of these, six EMC-dependent and six EMC-independent proteins were further independently validated. We found that a common feature among EMC-dependent proteins is that they contain transmembrane domains (TMDs) with polar and/or charged residues. Mutagenesis studies demonstrate that EMC dependency can be converted in cells by removing or introducing polar and/or charged residues within TMDs. Our studies expand the list of validated EMC-dependent and EMC-independent proteins and suggest that the EMC is involved in handling TMDs with residues challenging for membrane integration.
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