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TitleDirect visualization of degradation microcompartments at the ER membrane.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 2, Page 1069-1080, Year 2020
Publish dateJan 14, 2020
AuthorsSahradha Albert / Wojciech Wietrzynski / Chia-Wei Lee / Miroslava Schaffer / Florian Beck / Jan M Schuller / Patrice A Salomé / Jürgen M Plitzko / Wolfgang Baumeister / Benjamin D Engel /
PubMed AbstractTo 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:31882451 / PubMed Central
MethodsEM (tomography) / EM (subtomogram averaging)
Resolution17.24 - 35.0 Å
Structure data

EMDB-10409:
In situ cryo-electron tomogram from Chlamydomonas reinhardtii of a proteasome cluster at the endoplasmic reticulum
Method: EM (tomography)

EMDB-10410:
In situ subtomogram average of Chlamydomonas Cdc48 (C6 symmetry)
Method: EM (subtomogram averaging) / Resolution: 32.8 Å

EMDB-10411:
In situ subtomogram average of Chlamydomonas Cdc48 (C1 symmetry)
Method: EM (subtomogram averaging) / Resolution: 35.0 Å

EMDB-3932:
In situ subtomogram average of the Chlamydomonas double-capped 26S proteasome
Method: EM (subtomogram averaging) / Resolution: 21.88 Å

EMDB-3933:
In situ subtomogram average of the Chlamydomonas single-capped 26S proteasome
Method: EM (subtomogram averaging) / Resolution: 23.81 Å

EMDB-3934:
In situ subtomogram average of the Chlamydomonas ground state 26S proteasome
Method: EM (subtomogram averaging) / Resolution: 17.24 Å

EMDB-3935:
In situ subtomogram average of the Chlamydomonas processing state 26S proteasome
Method: EM (subtomogram averaging) / Resolution: 19.61 Å

Source
  • Chlamydomonas reinhardtii (plant)

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