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Verfasst von:Albert, Sahradha [VerfasserIn]   i
 Beck, Martin [VerfasserIn]   i
Titel:Proteasomes tether to two distinct sites at the nuclear pore complex
Verf.angabe:Sahradha Albert, Miroslava Schaffer, Florian Beck, Shyamal Mosalaganti, Shoh Asano, Henry F. Thomas, Jürgen M. Plitzko, Martin Beck, Wolfgang Baumeister, Benjamin D. Engel
E-Jahr:2017
Jahr:December 26, 2017
Umfang:6 S.
Teil:volume:114
 year:2017
 number:52
 pages:13726-13731
 extent:6
Fussnoten:Gesehen am 08.10.2018 ; Published ahead of print December 11, 2017
Titel Quelle:Enthalten in: National Academy of Sciences (Washington, DC)Proceedings of the National Academy of Sciences of the United States of America
Ort Quelle:Washington, DC : National Acad. of Sciences, 1915
Jahr Quelle:2017
Band/Heft Quelle:114(2017), 52, Seite 13726-13731
ISSN Quelle:1091-6490
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.
DOI:doi:10.1073/pnas.1716305114
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Kostenfrei: Volltext ; Verlag: http://dx.doi.org/10.1073/pnas.1716305114
 Kostenfrei: Volltext: http://www.pnas.org/content/114/52/13726
 DOI: https://doi.org/10.1073/pnas.1716305114
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:cryo-electron tomography
 focused ion beam
 nuclear pore complex
 proteasome
 quality control
K10plus-PPN:1581632282
Verknüpfungen:→ Zeitschrift

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