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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Late Embryogenesis Abundant Protein-Client Protein Interactions

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Autor(es):
Dirk, Lynnette M. A. [1] ; Abdel, Caser Ghaafar [2] ; Ahmad, Imran [3] ; Silva Neta, Izabel Costa [4] ; Pereira, Cristiane Carvalho [5] ; Carlos Bezerra Pereira, Francisco Elder [6] ; Uneda-Trevisoli, Sandra Helena [7] ; Pinheiro, Daniel Guariz [8] ; Downie, Allan Bruce [1]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] Univ Kentucky, Seed Biol Program, Dept Hort, Plant Sci Bldg, 1405 Vet Dr, Lexington, KY 40546 - USA
[2] Al Muthanna Univ, Agr Coll, Al Muthanna 66001 - Iraq
[3] Univ Agr, Fac Crop Prod Sci, Dept Hort, Peshawar 25120, Khyber Pakhtunk - Pakistan
[4] Agroceres Inc, BR-38703240 Patos De Minas, MG - Brazil
[5] Univ Fed Lavras, Dept Agr, Setor Sementes, BR-37200000 Lavras, MG - Brazil
[6] Germisul Ltd, BR-79108011 Campo Grande, MS - Brazil
[7] Natl Univ Sao Paulo, Dept Vegetable Prod, UNESP, BR-14884900 Jaboticabal, SP - Brazil
[8] Univ Sao Paulo, Fac Philosophy Sci & Letters Ribeirao Preto, Dept Biol, BR-14040901 Ribeirao Preto, SP - Brazil
Número total de Afiliações: 8
Tipo de documento: Artigo de Revisão
Fonte: PLANTS-BASEL; v. 9, n. 7 JUL 2020.
Citações Web of Science: 1
Resumo

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. (AU)

Processo FAPESP: 15/26238-9 - Identificação e análise funcional de proteínas LEA dehidrinas ortólogas de Arabidopsis e soja.
Beneficiário:Sandra Helena Unêda-Trevisoli
Linha de fomento: Bolsas no Exterior - Pesquisa