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  Structural disorder and its role in proteasomal degradation

Aufderheide, A., Unverdorben, P., Baumeister, W., & Förster, F. (2015). Structural disorder and its role in proteasomal degradation. FEBS Letters. Special Issue: Dynamics, flexibility, and intrinsic disorder in protein assemblies, 589(19, Part A), 2552-2560. doi:10.1016/j.febslet.2015.07.034.

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 Creators:
Aufderheide, Antje1, Author              
Unverdorben, Pia1, Author              
Baumeister, Wolfgang1, Author              
Förster, Friedrich2, 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              

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Free keywords: PROTEIN HALF-LIFE; 26 S PROTEASOME; SACCHAROMYCES-CEREVISIAE; DEUBIQUITINATING ENZYME; REGULATORY PARTICLE; 20S PROTEASOME; MOLECULAR ARCHITECTURE; SUBSTRATE DEGRADATION; MEDIATED PROTEOLYSIS; UBIQUITIN RECEPTORS26S proteasome; Proteostasis; Protein degradation; Disordered protein segment; Structural variability; Low complexity region;
 Abstract: The ubiquitin proteasome system is responsible for the controlled degradation of a vast number of intracellular proteins. It targets misfolded or otherwise aberrant proteins as well as proteins no longer needed at a given point in time. The 26S proteasome is a large macromolecular machine comprising 33 distinct subunits as well as a number of transiently associating cofactors. Being essentially a non-specific protease, specificity is conferred by the ubiquitin system, which selects and marks substrates for degradation. Here, we review our current understanding of the structure and function of the 26S proteasome; in doing so we highlight the role of disordered protein regions. Disordered segments in substrates promote their degradation, whereas low complexity regions prevent their proteolysis. In the 26S proteasome itself a main role of disordered segments seems to be rendering the ubiquitin receptors mobile, possibly supporting recruitment of polyubiquity-lated substrates. Thus, these structural features of substrates as well as of the 26S proteasome itself likely play important roles at different stages of the protein degradation process. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2015-09-14
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters. Special Issue: Dynamics, flexibility, and intrinsic disorder in protein assemblies
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 589 (19, Part A) Sequence Number: - Start / End Page: 2552 - 2560 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501