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Late Embryogenesis Abundant Protein–Client Protein Interactions

The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs prov...

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Autores principales: Dirk, Lynnette M. A., Abdel, Caser Ghaafar, Ahmad, Imran, Neta, Izabel Costa Silva, Pereira, Cristiane Carvalho, Pereira, Francisco Elder Carlos Bezerra, Unêda-Trevisoli, Sandra Helena, Pinheiro, Daniel Guariz, Downie, Allan Bruce
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412488/
https://www.ncbi.nlm.nih.gov/pubmed/32610443
http://dx.doi.org/10.3390/plants9070814
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author Dirk, Lynnette M. A.
Abdel, Caser Ghaafar
Ahmad, Imran
Neta, Izabel Costa Silva
Pereira, Cristiane Carvalho
Pereira, Francisco Elder Carlos Bezerra
Unêda-Trevisoli, Sandra Helena
Pinheiro, Daniel Guariz
Downie, Allan Bruce
author_facet Dirk, Lynnette M. A.
Abdel, Caser Ghaafar
Ahmad, Imran
Neta, Izabel Costa Silva
Pereira, Cristiane Carvalho
Pereira, Francisco Elder Carlos Bezerra
Unêda-Trevisoli, Sandra Helena
Pinheiro, Daniel Guariz
Downie, Allan Bruce
author_sort Dirk, Lynnette M. A.
collection PubMed
description The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs providing a shield molecule function, possibly by instigating liquid-liquid phase separations. Some LEAPs bind directly to their client proteins, exerting a holdase-type chaperonin function. Finally, instances of LEAP–client protein interactions have been documented, where the LEAP modulates (interferes with) the function of the client protein, acting as a surreptitious rheostat of cellular homeostasis. From the examples identified to date, it is apparent that client protein modulation also serves to mitigate stress. While some LEAPs can physically bind and protect client proteins, some apparently bind to assist the degradation of the client proteins with which they associate. Documented instances of LEAP–client protein binding, even in the absence of stress, brings to the fore the necessity of identifying how the LEAPs are degraded post-stress to render them innocuous, a first step in understanding how the cell regulates their abundance.
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spelling pubmed-74124882020-08-26 Late Embryogenesis Abundant Protein–Client Protein Interactions Dirk, Lynnette M. A. Abdel, Caser Ghaafar Ahmad, Imran Neta, Izabel Costa Silva Pereira, Cristiane Carvalho Pereira, Francisco Elder Carlos Bezerra Unêda-Trevisoli, Sandra Helena Pinheiro, Daniel Guariz Downie, Allan Bruce Plants (Basel) Review The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs providing a shield molecule function, possibly by instigating liquid-liquid phase separations. Some LEAPs bind directly to their client proteins, exerting a holdase-type chaperonin function. Finally, instances of LEAP–client protein interactions have been documented, where the LEAP modulates (interferes with) the function of the client protein, acting as a surreptitious rheostat of cellular homeostasis. From the examples identified to date, it is apparent that client protein modulation also serves to mitigate stress. While some LEAPs can physically bind and protect client proteins, some apparently bind to assist the degradation of the client proteins with which they associate. Documented instances of LEAP–client protein binding, even in the absence of stress, brings to the fore the necessity of identifying how the LEAPs are degraded post-stress to render them innocuous, a first step in understanding how the cell regulates their abundance. MDPI 2020-06-29 /pmc/articles/PMC7412488/ /pubmed/32610443 http://dx.doi.org/10.3390/plants9070814 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
Dirk, Lynnette M. A.
Abdel, Caser Ghaafar
Ahmad, Imran
Neta, Izabel Costa Silva
Pereira, Cristiane Carvalho
Pereira, Francisco Elder Carlos Bezerra
Unêda-Trevisoli, Sandra Helena
Pinheiro, Daniel Guariz
Downie, Allan Bruce
Late Embryogenesis Abundant Protein–Client Protein Interactions
title Late Embryogenesis Abundant Protein–Client Protein Interactions
title_full Late Embryogenesis Abundant Protein–Client Protein Interactions
title_fullStr Late Embryogenesis Abundant Protein–Client Protein Interactions
title_full_unstemmed Late Embryogenesis Abundant Protein–Client Protein Interactions
title_short Late Embryogenesis Abundant Protein–Client Protein Interactions
title_sort late embryogenesis abundant protein–client protein interactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412488/
https://www.ncbi.nlm.nih.gov/pubmed/32610443
http://dx.doi.org/10.3390/plants9070814
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