Modelling Proteasome and Proteasome Regulator Activities
Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes. Which cleavage sites are used within the target proteins and how fast these proteins are degraded have a profound impact on immune sy...
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pubmed-41014992014-07-28 Modelling Proteasome and Proteasome Regulator Activities Liepe, Juliane Holzhütter, Herman-Georg Kloetzel, Peter M. Stumpf, Michael P. H. Mishto, Michele Review Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes. Which cleavage sites are used within the target proteins and how fast these proteins are degraded have a profound impact on immune system function and many cellular metabolic processes. The regulation of proteasome activity involves different mechanisms, such as the substitution of the catalytic subunits, the binding of regulatory complexes to proteasome gates and the proteasome conformational modifications triggered by the target protein itself. Mathematical models are invaluable in the analysis; and potentially allow us to predict the complex interactions of proteasome regulatory mechanisms and the final outcomes of the protein degradation rate and MHC class I epitope generation. The pioneering attempts that have been made to mathematically model proteasome activity, cleavage preference variation and their modification by one of the regulatory mechanisms are reviewed here. MDPI 2014-06-20 /pmc/articles/PMC4101499/ /pubmed/24970232 http://dx.doi.org/10.3390/biom4020585 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Liepe, Juliane Holzhütter, Herman-Georg Kloetzel, Peter M. Stumpf, Michael P. H. Mishto, Michele |
spellingShingle |
Liepe, Juliane Holzhütter, Herman-Georg Kloetzel, Peter M. Stumpf, Michael P. H. Mishto, Michele Modelling Proteasome and Proteasome Regulator Activities |
author_facet |
Liepe, Juliane Holzhütter, Herman-Georg Kloetzel, Peter M. Stumpf, Michael P. H. Mishto, Michele |
author_sort |
Liepe, Juliane |
title |
Modelling Proteasome and Proteasome Regulator Activities |
title_short |
Modelling Proteasome and Proteasome Regulator Activities |
title_full |
Modelling Proteasome and Proteasome Regulator Activities |
title_fullStr |
Modelling Proteasome and Proteasome Regulator Activities |
title_full_unstemmed |
Modelling Proteasome and Proteasome Regulator Activities |
title_sort |
modelling proteasome and proteasome regulator activities |
description |
Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes. Which cleavage sites are used within the target proteins and how fast these proteins are degraded have a profound impact on immune system function and many cellular metabolic processes. The regulation of proteasome activity involves different mechanisms, such as the substitution of the catalytic subunits, the binding of regulatory complexes to proteasome gates and the proteasome conformational modifications triggered by the target protein itself. Mathematical models are invaluable in the analysis; and potentially allow us to predict the complex interactions of proteasome regulatory mechanisms and the final outcomes of the protein degradation rate and MHC class I epitope generation. The pioneering attempts that have been made to mathematically model proteasome activity, cleavage preference variation and their modification by one of the regulatory mechanisms are reviewed here. |
publisher |
MDPI |
publishDate |
2014 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4101499/ |
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1613115010923364352 |