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  Emerging mechanistic insights into AAA complexes regulating proteasomal degradation.

Förster, F., Schuller, J. M., Unverdorben, P., & Aufderheide, A. (2014). Emerging mechanistic insights into AAA complexes regulating proteasomal degradation. Biomolecules, 4(3), 774-794. doi:10.3390/biom4030774.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-AF47-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-AF48-3
Genre: Journal Article

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 Creators:
Förster, Friedrich1, Author              
Schuller, Jan M.1, Author              
Unverdorben, Pia1, Author              
Aufderheide, Antje2, Author              
Affiliations:
1Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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 Abstract: The 26S proteasome is an integral element of the ubiquitin-proteasome system(UPS) and, as such, responsible for regulated degradation of proteins in eukaryotic cells.It consists of the core particle, which catalyzes the proteolysis of substrates into small peptides, and the regulatory particle, which ensures specificity for a broad range of substrates.The heart of the regulatory particle is an AAA-ATPase unfoldase, which is surrounded by non-ATPase subunits enabling substrate recognition and processing. Cryo-EM-based studies revealed the molecular architecture of the 26S proteasome and its conformational rearrangements, providing insights into substrate recognition, commitment, deubiquitylation and unfolding. The cytosol proteasomal degradation of polyubiquitylated substrates is tuned by various associating cofactors, including deubiquitylating enzymes, ubiquitin ligases,shuttling ubiquitin receptors and the AAA-ATPase Cdc48/p97. Cdc48/p97 and its cofactors function upstream of the 26S proteasome, and their modular organization exhibits some striking analogies to the regulatory particle. In archaea PAN, the closest regulatory particle homolog and Cdc48 even have overlapping functions, underscoring their intricate relationship.Here, we review recent insights into the structure and dynamics of the 26S proteasome and its associated machinery, as well as our current structural knowledge on the Cdc48/p97 and its cofactors that function in the ubiquitin-proteasome system (UPS).

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 25102382
DOI: 10.3390/biom4030774
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Title: Biomolecules
  Alternative Title : Special Issue: Proteasomes and Its Regulators
Source Genre: Journal
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Publ. Info: Basel : MDPI
Pages: - Volume / Issue: 4 (3) Sequence Number: - Start / End Page: 774 - 794 Identifier: ISSN: 2218-273X