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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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Albert, Sahradha1, Autor           
Wietrzynski, Wojciech1, Autor           
Lee, Chia-Wei1, Autor           
Schaffer, Miroslava1, Autor           
Beck, Florian1, Autor           
Schuller, Jan M.2, Autor           
Salome, Patrice A.3, Autor
Plitzko, Jürgen M.1, Autor           
Baumeister, Wolfgang1, Autor           
Engel, Benjamin D.1, Autor           
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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Schlagwörter: 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;
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2020
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000508976200044
DOI: 10.1073/pnas.1905641117
 Art des Abschluß: -

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Titel: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Seiten: - Band / Heft: 117 (2) Artikelnummer: - Start- / Endseite: 1069 - 1080 Identifikator: ISSN: 0027-8424