Structural insights into the membrane chaperones for multi-pass membrane protein biogenesis |
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| Affiliation: | 1. Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing, 100083, China;2. Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, 49503, United States;1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA;2. Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, 97239, USA;1. Howard Hughes Medical Institute, University of Virginia School of Medicine, Charlottesville, VA, USA;2. Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, 480 Ray C. Hunt Dr., Charlottesville, VA 22908, USA;1. Department of Data Science and Artificial Intelligence, Faculty of Information Technology, Monash University, Clayton, 3800, Victoria, Australia;2. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, 16802, Pennsylvania, USA;1. Department of Biological Chemistry, University of California Los Angeles, 615 Charles E.Young Drive South, Los Angeles, CA 90095, USA;2. Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, CA 90095, USA;3. Department of Physiology, University of California Los Angeles, 615 Charles E. Young Drive South, Los Angeles, CA 90095, USA |
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| Abstract: | Certain transmembrane α-helices of multi-pass membrane proteins line substrate transport paths or catalytic pockets and, therefore, are partially hydrophilic. Sec61 alone is insufficient to insert these less hydrophobic segments into the membrane and needs to work with dedicated membrane chaperones. Three such membrane chaperones have been described in the literature—the endoplasmic reticulum membrane protein complex (EMC), the TMCO1 complex, and the PAT complex. Recent structural studies on these membrane chaperones have revealed their overall architecture, multi-subunit assembly, putative substrate transmembrane helix-binding pockets, and cooperative mechanisms with the ribosome and Sec61 translocon. These structures are providing initial insights into the poorly understood processes of multi-pass membrane protein biogenesis. |
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