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...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-06-01
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| Series: | Plants |
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| Online Access: | https://www.mdpi.com/2223-7747/9/7/814 |
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| author | Lynnette M. A. Dirk Caser Ghaafar Abdel Imran Ahmad Izabel Costa Silva Neta Cristiane Carvalho Pereira Francisco Elder Carlos Bezerra Pereira Sandra Helena Unêda-Trevisoli Daniel Guariz Pinheiro Allan Bruce Downie |
| author_facet | Lynnette M. A. Dirk Caser Ghaafar Abdel Imran Ahmad Izabel Costa Silva Neta Cristiane Carvalho Pereira Francisco Elder Carlos Bezerra Pereira Sandra Helena Unêda-Trevisoli Daniel Guariz Pinheiro Allan Bruce Downie |
| author_sort | Lynnette M. A. Dirk |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T18:49:09Z |
| format | Article |
| id | doaj.art-28edbf4b875842edbc2f4859c8b2d800 |
| institution | Directory Open Access Journal |
| issn | 2223-7747 |
| language | English |
| last_indexed | 2024-03-10T18:49:09Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Plants |
| spelling | doaj.art-28edbf4b875842edbc2f4859c8b2d8002023-11-20T05:14:58ZengMDPI AGPlants2223-77472020-06-019781410.3390/plants9070814Late Embryogenesis Abundant Protein–Client Protein InteractionsLynnette M. A. Dirk0Caser Ghaafar Abdel1Imran Ahmad2Izabel Costa Silva Neta3Cristiane Carvalho Pereira4Francisco Elder Carlos Bezerra Pereira5Sandra Helena Unêda-Trevisoli6Daniel Guariz Pinheiro7Allan Bruce Downie8Department of Horticulture, University of Kentucky Seed Biology Program, Plant Science Building, 1405 Veterans Drive, University of Kentucky, Lexington, KY 40546-0312, USAAgriculture College, Al-Muthanna University, Samawah, Al-Muthanna 66001, IraqDepartment of Horticulture, Faculty of Crop Production Sciences, The University of Agriculture, Peshawar, Khyber Pakhtunkhwa 25120, PakistanAgroceres, Inc., Patos de Minas, Minas Gerais CEP: 38703-240, BrazilDepartamento de Agricultura—Setor de Sementes, Federal University of Lavras, Lavras, Minas Gerais CEP: 37200-000, BrazilGermisul Ltd., Campo Grande, Mato Grosso do Sul CEP: 79108-011, BrazilDepartment of Vegetable Production, (UNESP) National University of São Paulo, Jaboticabal, São Paulo CEP: 14884-900, BrazilDepartment of Biology, Faculty of Philosophy, Science and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo CEP: 14040-901, BrazilDepartment of Horticulture, University of Kentucky Seed Biology Program, Plant Science Building, 1405 Veterans Drive, University of Kentucky, Lexington, KY 40546-0312, USAThe 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.https://www.mdpi.com/2223-7747/9/7/814late embryogenesis abundantprotein interactiondesiccationseednatural protection and repair mechanismstress |
| spellingShingle | Lynnette M. A. Dirk Caser Ghaafar Abdel Imran Ahmad Izabel Costa Silva Neta Cristiane Carvalho Pereira Francisco Elder Carlos Bezerra Pereira Sandra Helena Unêda-Trevisoli Daniel Guariz Pinheiro Allan Bruce Downie Late Embryogenesis Abundant Protein–Client Protein Interactions Plants late embryogenesis abundant protein interaction desiccation seed natural protection and repair mechanism stress |
| 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 | late embryogenesis abundant protein interaction desiccation seed natural protection and repair mechanism stress |
| url | https://www.mdpi.com/2223-7747/9/7/814 |
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