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Adaptation of Proteasomes and Lysosomes to Cellular Environments

Protein degradation is important for proper cellular physiology as it removes malfunctioning proteins or can provide a source for energy. Proteasomes and lysosomes, through the regulatory particles or adaptor proteins, respectively, recognize proteins destined for degradation. These systems have dev...

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Autores principales: Mebratu, Yohannes Afework, Negasi, Zerihun Hailemariam, Dutta, Saugata, Rojas-Quintero, Joselyn, Tesfaigzi, Yohannes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7600607/
https://www.ncbi.nlm.nih.gov/pubmed/33019542
http://dx.doi.org/10.3390/cells9102221
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author Mebratu, Yohannes Afework
Negasi, Zerihun Hailemariam
Dutta, Saugata
Rojas-Quintero, Joselyn
Tesfaigzi, Yohannes
author_facet Mebratu, Yohannes Afework
Negasi, Zerihun Hailemariam
Dutta, Saugata
Rojas-Quintero, Joselyn
Tesfaigzi, Yohannes
author_sort Mebratu, Yohannes Afework
collection PubMed
description Protein degradation is important for proper cellular physiology as it removes malfunctioning proteins or can provide a source for energy. Proteasomes and lysosomes, through the regulatory particles or adaptor proteins, respectively, recognize proteins destined for degradation. These systems have developed mechanisms to allow adaptation to the everchanging environment of the cell. While the complex recognition of proteins to be degraded is somewhat understood, the mechanisms that help switch the proteasomal regulatory particles or lysosomal adaptor proteins to adjust to the changing landscape of degrons, during infections or inflammation, still need extensive exploration. Therefore, this review is focused on describing the protein degradation systems and the possible sensors that may trigger the rapid adaptation of the protein degradation machinery.
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spelling pubmed-76006072020-11-01 Adaptation of Proteasomes and Lysosomes to Cellular Environments Mebratu, Yohannes Afework Negasi, Zerihun Hailemariam Dutta, Saugata Rojas-Quintero, Joselyn Tesfaigzi, Yohannes Cells Review Protein degradation is important for proper cellular physiology as it removes malfunctioning proteins or can provide a source for energy. Proteasomes and lysosomes, through the regulatory particles or adaptor proteins, respectively, recognize proteins destined for degradation. These systems have developed mechanisms to allow adaptation to the everchanging environment of the cell. While the complex recognition of proteins to be degraded is somewhat understood, the mechanisms that help switch the proteasomal regulatory particles or lysosomal adaptor proteins to adjust to the changing landscape of degrons, during infections or inflammation, still need extensive exploration. Therefore, this review is focused on describing the protein degradation systems and the possible sensors that may trigger the rapid adaptation of the protein degradation machinery. MDPI 2020-10-01 /pmc/articles/PMC7600607/ /pubmed/33019542 http://dx.doi.org/10.3390/cells9102221 Text en © 2020 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Mebratu, Yohannes Afework
Negasi, Zerihun Hailemariam
Dutta, Saugata
Rojas-Quintero, Joselyn
Tesfaigzi, Yohannes
Adaptation of Proteasomes and Lysosomes to Cellular Environments
title Adaptation of Proteasomes and Lysosomes to Cellular Environments
title_full Adaptation of Proteasomes and Lysosomes to Cellular Environments
title_fullStr Adaptation of Proteasomes and Lysosomes to Cellular Environments
title_full_unstemmed Adaptation of Proteasomes and Lysosomes to Cellular Environments
title_short Adaptation of Proteasomes and Lysosomes to Cellular Environments
title_sort adaptation of proteasomes and lysosomes to cellular environments
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7600607/
https://www.ncbi.nlm.nih.gov/pubmed/33019542
http://dx.doi.org/10.3390/cells9102221
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