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Proteolysis and Proteolytic Enzymes

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 1250

Special Issue Editor

Institute of Molecular Genetics of National Research Centre “Kurchatov Institute”, Moscow 123182, Russia
Interests: proteolytic enzymes; protein protease inhibitor; proteolytic regulation

Special Issue Information

Dear Colleagues,

Proteolysis is a fundamental regulatory mechanism critical for all living systems. The significance of proteolysis seems evident, and studies on proteolytic enzymes have a long and rich history. Yet, our knowledge about the function of proteases in cells and organisms is limited. It is no exaggeration to say that the biological function even of characterized proteolytic enzymes remains largely unclear. At the same time, the available data suggest that proteolysis and its dysregulation are significant factors in many pathologies. Accordingly, studies of proteolytic enzymes, proteolysis regulation, and proteolysis as regulatory factors are vital to understanding the mechanisms of pathogenesis and finding new therapeutic strategies.

The goal of this Special Issue is to present new data on proteases and discuss a broad range of their functional aspects including the proteolytic regulation, regulation of proteolysis, protease involvement in physiological and pathological processes, structural and functional relationships in their molecules, and functions of protease inhibitors. Both original studies and reviews by experts in the field are welcomed.

Dr. Ilya V. Demidyuk
Guest Editor

This special issue is assisted by Topical Advisory Panel Member Dr. Alexey Komissarov (Institute of Molecular Genetics of National Research Center "Kurchatov Institute").

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • proteolysis
  • protease
  • protease inhibitor
  • proteolytic regulation
  • regulation of proteolysis
  • proteolytic processing
  • protein degradation

Published Papers (1 paper)

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Research

19 pages, 5988 KiB  
Article
Brain-Derived 11S Regulator (PA28αβ) Promotes Proteasomal Hydrolysis of Elongated Oligoglutamine-Containing Peptides
by Viacheslav A. Kriachkov, Natalia N. Gotmanova, Vadim N. Tashlitsky and Anna V. Bacheva
Int. J. Mol. Sci. 2023, 24(17), 13275; https://doi.org/10.3390/ijms241713275 - 26 Aug 2023
Viewed by 744
Abstract
Proteins with extended polyglutamine regions are associated with several neurodegenerative disorders, including Huntington’s disease. Intracellular proteolytic processing of these proteins is not well understood. In particular, it is unclear whether long polyglutamine fragments resulting from the proteolysis of these proteins can be potentially [...] Read more.
Proteins with extended polyglutamine regions are associated with several neurodegenerative disorders, including Huntington’s disease. Intracellular proteolytic processing of these proteins is not well understood. In particular, it is unclear whether long polyglutamine fragments resulting from the proteolysis of these proteins can be potentially cleaved by the proteasome. Here, we studied the susceptibility of the glutamine-glutamine bond to proteolysis by the proteasome using oligoglutamine-containing peptides with a fluorophore/quencher pair. We found that the addition of the 11S proteasomal regulator (also known as PA28) significantly accelerated the hydrolysis of oligoglutamine-containing peptides by the 20S proteasome. Unexpectedly, a similar effect was observed for the 26S proteasome in the presence of the 11S regulator. LC/MS data revealed that the hydrolysis of our peptides with both 20S and 26S proteasomes leads to N-terminal fragments containing two or three glutamine residues and that the hydrolysis site does not change after the addition of the 11S regulator. This was confirmed by the docking experiment, which shows that the preferred hydrolysis site is located after the second/third glutamine residue. Inhibitory analysis revealed that trypsin-like specificity is mainly responsible for the proteasomal hydrolysis of the glutamine-glutamine bond. Together, our results indicate that both 20S and 26S proteasomes are capable of degrading the N-terminal part of oligoglutamine fragments, while the 11S regulator significantly accelerates the hydrolysis without changing its specificity. This data suggests that proteasome activity may be enhanced in relation to polyglutamine substrates present in neurons in the early stages of polyglutamine disorders. Full article
(This article belongs to the Special Issue Proteolysis and Proteolytic Enzymes)
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