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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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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-6F11-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-6F12-0
Genre: Journal Article

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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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 Creators:
Albert, Sahradha1, Author              
Schaffer, Miroslava1, Author              
Beck, Florian1, Author              
Mosalaganti, Shyamal2, Author
Asano, Shoh1, Author              
Thomas, Henry F.1, Author              
Plitzko, Jürgen M.1, Author              
Beck, Martin2, Author
Baumeister, Wolfgang1, Author              
Engel, Benjamin D.1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: 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;
 Abstract: 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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Language(s): eng - English
 Dates: 2017-12-262017
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000418722400059
DOI: 10.1073/pnas.1716305114
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (52) Sequence Number: - Start / End Page: 13726 - 13731 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230