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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Proteasomes tether to two distinct sites at the nuclear pore complex.
Proc. Natl. Acad. Sci. U.S.A. 114, 13726-13731 (2017)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cryo-electron Tomography ; Focused Ion Beam ; Nuclear Pore Complex ; Proteasome ; Quality Control
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Volume: 114,
Issue: 52,
Pages: 13726-13731
Publisher
National Academy of Sciences
Reviewing status
Peer reviewed
Institute(s)
Helmholtz Pioneer Campus (HPC)