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  Direct visualization of degradation microcompartments at the ER membrane

Albert, S., Wietrzynski, W., Lee, C.-W., Schaffer, M., Beck, F., Schuller, J. M., et al. (2020). Direct visualization of degradation microcompartments at the ER membrane. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 117(2), 1069-1080. doi:10.1073/pnas.1905641117.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-C742-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-C78D-C
Genre: Journal Article

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 Creators:
Albert, Sahradha1, Author              
Wietrzynski, Wojciech1, Author              
Lee, Chia-Wei1, Author              
Schaffer, Miroslava1, Author              
Beck, Florian1, Author              
Schuller, Jan M.2, Author              
Salome, Patrice A.3, Author
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Engel, Benjamin D.1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3external, ou_persistent22              

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Free keywords: RETICULUM-ASSOCIATED DEGRADATION; UNFOLDED PROTEIN RESPONSE; CRYO-EM STRUCTURE; ENDOPLASMIC-RETICULUM; PHASE-SEPARATION; CRYOELECTRON TOMOGRAMS; LIQUID-LIKE; PROTEASOME; REVEALS; LOCALIZATIONproteasome; cdc48; ERAD; phase separation; cryo-electron tomography;
 Abstract: To promote the biochemical reactions of life, cells can compartmentalize molecular interaction partners together within separated non-membrane-bound regions. It is unknown whether this strategy is used to facilitate protein degradation at specific locations within the cell. Leveraging in situ cryo-electron tomography to image the native molecular landscape of the unicellular alga Chlamydomonas reinhardtii, we discovered that the cytosolic protein degradation machinery is concentrated within similar to 200-nm foci that contact specialized patches of endoplasmic reticulum (ER) membrane away from the ER-Golgi interface. These non-membrane-bound microcompartments exclude ribosomes and consist of a core of densely clustered 265 proteasomes surrounded by a loose cloud of Cdc48. Active proteasomes in the microcompartments directly engage with putative substrate at the ER membrane, a function canonically assigned to Cdc48. Live-cell fluorescence microscopy revealed that the proteasome clusters are dynamic, with frequent assembly and fusion events. We propose that the microcompartments perform ER-associated degradation, colocalizing the degradation machinery at specific ER hot spots to enable efficient protein quality control.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000508976200044
DOI: 10.1073/pnas.1905641117
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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 117 (2) Sequence Number: - Start / End Page: 1069 - 1080 Identifier: ISSN: 0027-8424