English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  A molecular census of 26S proteasomes in intact neurons

Asano, S., Fukuda, Y., Beck, F., Aufderheide, A., Förster, F., Danev, R., et al. (2015). A molecular census of 26S proteasomes in intact neurons. SCIENCE, 347(6220), 439-442. doi:10.1126/science.1261197.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Asano, Shoh1, Author              
Fukuda, Yoshiyuki1, Author              
Beck, Florian1, Author              
Aufderheide, Antje1, Author              
Förster, Friedrich2, Author              
Danev, Radostin1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              

Content

show
hide
Free keywords: UBIQUITIN; ARCHITECTURE; CELL; CLASSIFICATION; SUBTOMOGRAMS; DEGRADATION; RESOLUTION; COMPLEX; SYSTEM
 Abstract: The 26S proteasome is a key player in eukaryotic protein quality control and in the regulation of numerous cellular processes. Here, we describe quantitative in situ structural studies of this highly dynamic molecular machine in intact hippocampal neurons. We used electron cryotomography with the Volta phase plate, which allowed high fidelity and nanometer precision localization of 26S proteasomes. We undertook a molecular census of single-and double-capped proteasomes and assessed the conformational states of individual complexes. Under the conditions of the experiment-that is, in the absence of proteotoxic stress-only 20% of the 26S proteasomes were engaged in substrate processing. The remainder was in the substrate-accepting ground state. These findings suggest that in the absence of stress, the capacity of the proteasome system is not fully used.

Details

show
hide
Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000348225800048
DOI: 10.1126/science.1261197
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: SCIENCE
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA : AMER ASSOC ADVANCEMENT SCIENCE
Pages: - Volume / Issue: 347 (6220) Sequence Number: - Start / End Page: 439 - 442 Identifier: ISSN: 0036-8075