Late embryogenesis abundant protein–client protein interactions

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of Kentucky-
Autor(es): dc.contributorAl-Muthanna University-
Autor(es): dc.contributorThe University of Agriculture-
Autor(es): dc.contributorInc.-
Autor(es): dc.contributorFederal University of Lavras-
Autor(es): dc.contributorGermisul Ltd.-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorDirk, Lynnette M. A.-
Autor(es): dc.creatorAbdel, Caser Ghaafar-
Autor(es): dc.creatorAhmad, Imran-
Autor(es): dc.creatorNeta, Izabel Costa Silva-
Autor(es): dc.creatorPereira, Cristiane Carvalho-
Autor(es): dc.creatorPereira, Francisco Elder Carlos Bezerra-
Autor(es): dc.creatorUnêda-Trevisoli, Sandra Helena [UNESP]-
Autor(es): dc.creatorPinheiro, Daniel Guariz-
Autor(es): dc.creatorDownie, Allan Bruce-
Data de aceite: dc.date.accessioned2022-02-22T00:26:20Z-
Data de disponibilização: dc.date.available2022-02-22T00:26:20Z-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-07-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/plants9070814-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/199049-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/199049-
Descrição: dc.descriptionThe 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.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionDepartment of Horticulture University of Kentucky Seed Biology University of Kentucky, Plant Science Building, 1405 Veterans Drive-
Descrição: dc.descriptionAgriculture College Al-Muthanna University-
Descrição: dc.descriptionDepartment of Horticulture Faculty of Crop Production Sciences The University of Agriculture-
Descrição: dc.descriptionAgroceres Inc.-
Descrição: dc.descriptionDepartamento de Agricultura—Setor de Sementes Federal University of Lavras-
Descrição: dc.descriptionGermisul Ltd.-
Descrição: dc.descriptionDepartment of Vegetable Production (UNESP) National University of São Paulo-
Descrição: dc.descriptionDepartment of Biology Faculty of Philosophy Science and Letters of Ribeirão Preto University of São Paulo-
Descrição: dc.descriptionDepartment of Vegetable Production (UNESP) National University of São Paulo-
Formato: dc.format1-35-
Idioma: dc.languageen-
Relação: dc.relationPlants-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectDesiccation-
Palavras-chave: dc.subjectLate embryogenesis abundant-
Palavras-chave: dc.subjectNatural protection and repair mechanism-
Palavras-chave: dc.subjectProtein interaction-
Palavras-chave: dc.subjectSeed-
Palavras-chave: dc.subjectStress-
Título: dc.titleLate embryogenesis abundant protein–client protein interactions-
Aparece nas coleções:Repositório Institucional - Unesp

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