Proteomic Analysis Identifies Membrane Proteins Dependent on the ER Membrane Protein Complex
Year: 2019
Type: article
Abstract: 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.
Source: Cell Reports
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,200
Awards: Molecular mechanism for retrograde transport of tetanus neurotoxin, Structure and Function of C. Difficile Toxins, Molecular basis of action and pathogenesis of Clostridium difficile toxin B, Intellectual and Developmental Disablities Research Center, Integrated Epithelial and Muscosal Biology, Biology and Engineering of Botulinum Neurotoxins.
OpenAlex ID: W2972136233