Late Embryogenesis Abundant Protein-Client Protein Interactions

Author(s)

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]

Affiliation

^[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

• Document type: Review article
• Source: PLANTS-BASEL; v. 9, n. 7 JUL 2020.
• Web of Science Citations: 1

Abstract

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)

• FAPESP's process: 15/26238-9 - Identification and functional analysis of Arabidopsis and soybean orthologous dehydrin LEA protein-interacting proteins.
• Grantee: Sandra Helena Unêda-Trevisoli
• Support Opportunities: Scholarships abroad - Research