How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell
The 26S proteasome is the central element of proteostasis regulation in eukaryotic cells, it is required for the degradation of protein factors in multiple cellular pathways and it plays a fundamental role in cell stability. The main aspects of proteasome mediated protein degradation have been highl...
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Format: | Article |
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MDPI AG
2019-08-01
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Series: | Biomolecules |
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Online Access: | https://www.mdpi.com/2218-273X/9/9/395 |
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author | Bernat Coll-Martínez Bernat Crosas |
author_facet | Bernat Coll-Martínez Bernat Crosas |
author_sort | Bernat Coll-Martínez |
collection | DOAJ |
description | The 26S proteasome is the central element of proteostasis regulation in eukaryotic cells, it is required for the degradation of protein factors in multiple cellular pathways and it plays a fundamental role in cell stability. The main aspects of proteasome mediated protein degradation have been highly (but not totally) described during three decades of intense cellular, molecular, structural and chemical biology research and tool development. Contributions accumulated within this time lapse allow researchers today to go beyond classical partial views of the pathway, and start generating almost complete views of how the proteasome acts inside the cell. These views have been recently reinforced by cryo-electron microscopy and mechanistic works that provide from landscapes of proteasomal populations distributed in distinct intracellular contexts, to detailed shots of each step of the process of degradation of a given substrate, of the factors that regulate it, and precise measurements of the speed of degradation. Here, we present an updated digest of the most recent developments that significantly contribute in our understanding of how the 26S proteasome degrades hundreds of ubiquitinated substrates in multiple intracellular environments. |
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id | doaj.art-b7894635ee2641d7a3c98e783f9376b1 |
institution | Directory Open Access Journal |
issn | 2218-273X |
language | English |
last_indexed | 2024-12-20T00:23:31Z |
publishDate | 2019-08-01 |
publisher | MDPI AG |
record_format | Article |
series | Biomolecules |
spelling | doaj.art-b7894635ee2641d7a3c98e783f9376b12022-12-21T20:00:08ZengMDPI AGBiomolecules2218-273X2019-08-019939510.3390/biom9090395biom9090395How the 26S Proteasome Degrades Ubiquitinated Proteins in the CellBernat Coll-Martínez0Bernat Crosas1Department of Cell Biology, Institute of Molecular Biology of Barcelona (IBMB), Consejo Superior de investigaciones Científicas (CSIC), Baldiri i Reixac 4-10, 08028 Barcelona, SpainDepartment of Cell Biology, Institute of Molecular Biology of Barcelona (IBMB), Consejo Superior de investigaciones Científicas (CSIC), Baldiri i Reixac 4-10, 08028 Barcelona, SpainThe 26S proteasome is the central element of proteostasis regulation in eukaryotic cells, it is required for the degradation of protein factors in multiple cellular pathways and it plays a fundamental role in cell stability. The main aspects of proteasome mediated protein degradation have been highly (but not totally) described during three decades of intense cellular, molecular, structural and chemical biology research and tool development. Contributions accumulated within this time lapse allow researchers today to go beyond classical partial views of the pathway, and start generating almost complete views of how the proteasome acts inside the cell. These views have been recently reinforced by cryo-electron microscopy and mechanistic works that provide from landscapes of proteasomal populations distributed in distinct intracellular contexts, to detailed shots of each step of the process of degradation of a given substrate, of the factors that regulate it, and precise measurements of the speed of degradation. Here, we present an updated digest of the most recent developments that significantly contribute in our understanding of how the 26S proteasome degrades hundreds of ubiquitinated substrates in multiple intracellular environments.https://www.mdpi.com/2218-273X/9/9/395ubiquitinproteasomeATPase motorprotein degradation mechanism |
spellingShingle | Bernat Coll-Martínez Bernat Crosas How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell Biomolecules ubiquitin proteasome ATPase motor protein degradation mechanism |
title | How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell |
title_full | How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell |
title_fullStr | How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell |
title_full_unstemmed | How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell |
title_short | How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell |
title_sort | how the 26s proteasome degrades ubiquitinated proteins in the cell |
topic | ubiquitin proteasome ATPase motor protein degradation mechanism |
url | https://www.mdpi.com/2218-273X/9/9/395 |
work_keys_str_mv | AT bernatcollmartinez howthe26sproteasomedegradesubiquitinatedproteinsinthecell AT bernatcrosas howthe26sproteasomedegradesubiquitinatedproteinsinthecell |