An unstructured proteasome inhibitor comes into focus

The inhibitory mechanism of an intrinsically disordered proteasome inhibitor identified over 30 years ago has finally been revealed by cryo-electron microscopy by Hsu et al. in a recent report in the Journal of Biological Chemistry. The structure, coupled with biochemical and cell-based experiments,...

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Detalles Bibliográficos
Autores principales: Nemec, Antonia A., Tomko, Robert J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2023
Materias:
Editors' Pick Highlight
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10463253/
https://www.ncbi.nlm.nih.gov/pubmed/37562568
http://dx.doi.org/10.1016/j.jbc.2023.105145
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author Nemec, Antonia A.
Tomko, Robert J.
author_facet Nemec, Antonia A.
Tomko, Robert J.
author_sort Nemec, Antonia A.
collection PubMed
description The inhibitory mechanism of an intrinsically disordered proteasome inhibitor identified over 30 years ago has finally been revealed by cryo-electron microscopy by Hsu et al. in a recent report in the Journal of Biological Chemistry. The structure, coupled with biochemical and cell-based experiments, resolves lingering questions about how the inhibitor achieves multisite inhibition of proteasomal protease activity, while raising several exciting new questions on the nature of proteasome subpopulations in the process.
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spelling pubmed-104632532023-08-30 An unstructured proteasome inhibitor comes into focus Nemec, Antonia A. Tomko, Robert J. J Biol Chem Editors' Pick Highlight The inhibitory mechanism of an intrinsically disordered proteasome inhibitor identified over 30 years ago has finally been revealed by cryo-electron microscopy by Hsu et al. in a recent report in the Journal of Biological Chemistry. The structure, coupled with biochemical and cell-based experiments, resolves lingering questions about how the inhibitor achieves multisite inhibition of proteasomal protease activity, while raising several exciting new questions on the nature of proteasome subpopulations in the process. American Society for Biochemistry and Molecular Biology 2023-08-09 /pmc/articles/PMC10463253/ /pubmed/37562568 http://dx.doi.org/10.1016/j.jbc.2023.105145 Text en © 2023 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Editors' Pick Highlight
Nemec, Antonia A.
Tomko, Robert J.
An unstructured proteasome inhibitor comes into focus
title An unstructured proteasome inhibitor comes into focus
title_full An unstructured proteasome inhibitor comes into focus
title_fullStr An unstructured proteasome inhibitor comes into focus
title_full_unstemmed An unstructured proteasome inhibitor comes into focus
title_short An unstructured proteasome inhibitor comes into focus
title_sort unstructured proteasome inhibitor comes into focus
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10463253/
https://www.ncbi.nlm.nih.gov/pubmed/37562568
http://dx.doi.org/10.1016/j.jbc.2023.105145
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