The Ubiquitin-Independent, 20S Proteasome-Mediated, Protein Degradation Pathway

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (31 December 2018) | Viewed by 326

Special Issue Editors


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Guest Editor
Weizmann Institute of Science Israel, Department of Biomolecular Sciences, Rehovot, Israel
Interests: structural biology; mass spectrometry; structure function relationship; protein complexes involved in the protein degradation pathway

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Guest Editor
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
Interests: intrinsically disordered proteins; ubiquitin independent proteasomal degradation; degradation by 20S proteasome; gene editing; the hepatitis B virus; DNA damage signaling

Special Issue Information

Dear Colleagues,

It is now increasingly evident that proteins undergo degradation by an ubiquitin-independent mechanism mediated by the 20S proteasome core itself. This proteolytic process is carried out without the regulatory task of the 19S particle and substrate selectivity achieved by ubiquitin tagging. To date, it is clear that a significant fraction of the 20S proteasomes are uncapped, and about 20% are associated with proteasome activators, such as the cytosolic PA28αβ (or 11S) and nuclear PA28γ and PA200, which enhance the proteolytic capacity of the complex in an ATP- and ubiquitin-independent manner. The composition and localization of these proteasome complexes is dynamically changing according to various stimuli or pathological contexts. Although initially believed to be limited to rare exceptions, the range of identified ubiquitin-independent 20S proteasome substrates is increasing, many of which are key regulatory proteins. Despite this progress in knowledge, many details concerning 20S proteolysis are still unknown, like what are the regulators, mediators, shuttle proteins and array of substrates degraded by this cellular pathway.

The purpose of this Special Issue is to provide a current overview of recent findings in the field of 20S-mediated degradation and to showcase original research in this important biological process. By bringing together the current work and views on 20S mediated ubiquitin-independent degradation, we aim to boost further exploration and better understanding of this cellular process. Submission of reviews and basic research papers are encouraged.

Dr. Michal Sharon
Prof. Yosef Shaul
Guest Editors

Manuscript Submission Information

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Keywords

  • 20S proteasome
  • ubiquitin independent protein degradation
  • intrinsically disordered proteins
  • oxidative stress
  • PA28αβ, PA28γ, PA200

Published Papers

There is no accepted submissions to this special issue at this moment.
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