Direct visualization of degradation microcompartments at the ER membrane

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.

doi:10.1073/pnas.1905641117

Direct visualization of degradation microcompartments at the ER membrane

Journal Article · Fri Dec 27 00:00:00 EST 2019 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1905641117· OSTI ID:1580556

Albert, Sahradha ^[1]; Wietrzynski, Wojciech ^[1]; Lee, Chia-Wei ^[1]; Schaffer, Miroslava ^[1]; Beck, Florian ^[1]; Schuller, Jan M. ^[2]; ^[3]; ^[1]; Baumeister, Wolfgang ^[1]; ^[1]

Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany,
Department of Structural Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany,
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095

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 ∼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.

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Research Organization:: Univ. of California, Los Angeles, CA (United States)

Sponsoring Organization:: USDOE; USDOE Office of Science (SC)

Grant/Contract Number:: FC02-02ER63421

OSTI ID:: 1580556

Alternate ID(s):: OSTI ID: 1625041

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 2 Vol. 117; ISSN 0027-8424

Publisher:: Proceedings of the National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: English

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