The Heat Shock Protein 40-Type Chaperone MASH Supports the Endoplasmic Reticulum-Associated Degradation E3 Ubiquitin Ligase MAKIBISHI1 in Medicago truncatula
| العنوان: | The Heat Shock Protein 40-Type Chaperone MASH Supports the Endoplasmic Reticulum-Associated Degradation E3 Ubiquitin Ligase MAKIBISHI1 in Medicago truncatula |
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| المؤلفون: | Marie-Laure Erffelinck, Bianca Ribeiro, Lore Gryffroy, Avanish Rai, Jacob Pollier, Alain Goossens |
| المصدر: | Frontiers in Plant Science FRONTIERS IN PLANT SCIENCE Frontiers in Plant Science, Vol 12 (2021) |
| بيانات النشر: | Frontiers Media SA, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, Plant Science, lcsh:Plant culture, Endoplasmic-reticulum-associated protein degradation, 01 natural sciences, 03 medical and health sciences, Ubiquitin, Heat shock protein, Arabidopsis, chaperone, lcsh:SB1-1110, protein quality control, triterpene saponin, E3-ubiquitin ligase, Original Research, biology, Chemistry, Endoplasmic reticulum, Biology and Life Sciences, food and beverages, biology.organism_classification, jasmonate, Medicago truncatula, RING membrane-anchor protein, Cell biology, Ubiquitin ligase, endoplasmic reticulum, 030104 developmental biology, 3-hydroxy-3-methylglutaryl-CoA reductase, Chaperone (protein), biology.protein, 010606 plant biology & botany |
| الوصف: | Jasmonates (JA) are oxylipin-derived phytohormones that trigger the production of specialized metabolites that often serve in defense against biotic stresses. InMedicago truncatula, a JA-induced endoplasmic reticulum-associated degradation (ERAD)-type machinery manages the production of bioactive triterpenes and thereby secures correct plant metabolism, growth, and development. This machinery involves the conserved RING membrane-anchor (RMA)-type E3 ubiquitin ligase MAKIBISHI1 (MKB1). Here, we discovered two additional members of this protein control apparatus via a yeast-based protein–protein interaction screen and characterized their function. First, a cognate E2 ubiquitin-conjugating enzyme was identified that interacts with MKB1 to deliver activated ubiquitin and to mediate its ubiquitination activity. Second, we identified a heat shock protein 40 (HSP40) that interacts with MKB1 to support its activity and was therefore designated MKB1-supporting HSP40 (MASH).MASHexpression was found to be co-regulated with that ofMKB1. The presence of MASH is critical for MKB1 and ERAD functioning because the dramatic morphological, transcriptional, and metabolic phenotype ofMKB1knock-downM. truncatulahairy roots was phenocopied by silencing ofMASH. Interaction was also observed between theArabidopsis thaliana(Arabidopsis) homologs of MASH and MKB1, suggesting that MASH represents an essential and plant-specific component of this vital and conserved eukaryotic protein quality control machinery. |
| وصف الملف: | application/pdf |
| تدمد: | 1664-462X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55edf5989ca309f421659e350492fadfTest https://doi.org/10.3389/fpls.2021.639625Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....55edf5989ca309f421659e350492fadf |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1664462X |
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