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Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder

Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are asso...

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Autores principales: Hong, Sunghyun, Choi, Sangmin, Kim, Ryeonghyeon, Koh, Junseock
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7700844/
https://www.ncbi.nlm.nih.gov/pubmed/33243935
http://dx.doi.org/10.14348/molcells.2020.0186
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author Hong, Sunghyun
Choi, Sangmin
Kim, Ryeonghyeon
Koh, Junseock
author_facet Hong, Sunghyun
Choi, Sangmin
Kim, Ryeonghyeon
Koh, Junseock
author_sort Hong, Sunghyun
collection PubMed
description Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research.
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spelling pubmed-77008442020-12-08 Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder Hong, Sunghyun Choi, Sangmin Kim, Ryeonghyeon Koh, Junseock Mol Cells Minireview Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research. Korean Society for Molecular and Cellular Biology 2020-11-30 2020-11-26 /pmc/articles/PMC7700844/ /pubmed/33243935 http://dx.doi.org/10.14348/molcells.2020.0186 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. https://creativecommons.org/licenses/by-nc-sa/3.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ (https://creativecommons.org/licenses/by-nc-sa/3.0/)
spellingShingle Minireview
Hong, Sunghyun
Choi, Sangmin
Kim, Ryeonghyeon
Koh, Junseock
Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title_full Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title_fullStr Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title_full_unstemmed Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title_short Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
title_sort mechanisms of macromolecular interactions mediated by protein intrinsic disorder
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7700844/
https://www.ncbi.nlm.nih.gov/pubmed/33243935
http://dx.doi.org/10.14348/molcells.2020.0186
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