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  Proteasomes tether to two distinct sites at the nuclear pore complex

Albert, S., Schaffer, M., Beck, F., Mosalaganti, S., Asano, S., Thomas, H. F., et al. (2017). Proteasomes tether to two distinct sites at the nuclear pore complex. Proceedings of the National Academy of Sciences of the United States of America, 114(52), 13726-13731. doi:10.1073/pnas.1716305114.

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Copyright © 2017 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
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Data deposition: Cryo-EM maps from subtomogram averaging, along with the tomogram shown in Fig. 1, were uploaded to the Electron Microscopy Data Bank, https://www.ebi.ac.uk/pdbe/emdb/ (accession nos. EMD-3932–EMD-3940 and EMD-3967).
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 Urheber:
Albert, Sahradha1, Autor           
Schaffer, Miroslava1, Autor           
Beck, Florian1, Autor           
Mosalaganti, Shyamal2, Autor
Asano, Shoh1, Autor           
Thomas, Henry F.1, Autor           
Plitzko, Jürgen M.1, Autor           
Beck, Martin2, 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              
2external, ou_persistent22              

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Schlagwörter: PROTEIN-QUALITY CONTROL; 26S PROTEASOME; CRYOELECTRON TOMOGRAPHY; STRUCTURAL-ANALYSIS; ELECTRON CRYOMICROSCOPY; CYTOSOLIC PROTEINS; MEMBRANE-PROTEINS; FISSION YEAST; LOCALIZATION; DEGRADATIONScience & Technology - Other Topics; proteasome; nuclear pore complex; quality control; focused ion beam; cryo-electron tomography;
 Zusammenfassung: The partitioning of cellular components between the nucleus and cytoplasm is the defining feature of eukaryotic life. The nuclear pore complex (NPC) selectively gates the transport of macromolecules between these compartments, but it is unknown whether surveillance mechanisms exist to reinforce this function. By leveraging in situ cryo-electron tomography to image the native cellular environment of Chlamydomonas reinhardtii, we observed that nuclear 26S proteasomes crowd around NPCs. Through a combination of subtomogram averaging and nanometer-precision localization, we identified two classes of proteasomes tethered via their Rpn9 subunits to two specific NPC locations: binding sites on the NPC basket that reflect its eightfold symmetry and more abundant binding sites at the inner nuclear membrane that encircle the NPC. These basket-tethered and membrane-tethered proteasomes, which have similar substrate-processing state frequencies as proteasomes elsewhere in the cell, are ideally positioned to regulate transcription and perform quality control of both soluble and membrane proteins transiting the NPC.

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Sprache(n): eng - English
 Datum: 2017-12-262017
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000418722400059
DOI: 10.1073/pnas.1716305114
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proceedings of the National Academy of Sciences of the USA
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 114 (52) Artikelnummer: - Start- / Endseite: 13726 - 13731 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230