Direct visualization of degradation microcompartments at the ER membrane.

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ID: 76115
2019
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Ranked #126 of 292 articles by views in Proceedings of the National Academy of Sciences of the United States of America

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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 , we discovered that the cytosolic protein degradation machinery is concentrated within ∼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 26S 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.
Reference Key
albert2019directproceedings Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Albert, Sahradha;Wietrzynski, Wojciech;Lee, Chia-Wei;Schaffer, Miroslava;Beck, Florian;Schuller, Jan M;Salomé, Patrice A;Plitzko, Jürgen M;Baumeister, Wolfgang;Engel, Benjamin D;
Journal Proceedings of the National Academy of Sciences of the United States of America
Year 2019
DOI
201905641
URL
Keywords
phase separation proteasome cryo-electron tomography erad cdc48

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