OsFes1C, a potential nucleotide exchange factor for OsBiP1, is involved in the ER and salt stress responses
| العنوان: | OsFes1C, a potential nucleotide exchange factor for OsBiP1, is involved in the ER and salt stress responses |
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| المؤلفون: | Le Qing Qu, Mei Li, Dandan Qian, Shuo Xiong, Lihong Tian |
| المصدر: | Plant Physiol |
| بيانات النشر: | Oxford University Press (OUP), 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, Physiology, Plant Science, Proteomics, Salt Stress, 01 natural sciences, Nucleotide exchange factor, 03 medical and health sciences, Organelle, Genetics, Research Articles, Plant Proteins, biology, Chemistry, Endoplasmic reticulum, food and beverages, Oryza, Endoplasmic Reticulum Stress, Cell biology, Cytosol, 030104 developmental biology, Chaperone (protein), biology.protein, Unfolded protein response, Binding immunoglobulin protein, Molecular Chaperones, 010606 plant biology & botany |
| الوصف: | The endoplasmic reticulum (ER) quality control system monitors protein homeostasis and relies on the activity of many molecular chaperones. Binding immunoglobulin protein (BiP) is a major ER luminal chaperone that is involved in most functions of the organelle. BiP activity is tightly regulated by nucleotide exchange factors (NEFs). However, information about NEFs in plants is limited. We obtained a Fes1-like protein (OsFes1C) through isobaric tags for relative and absolute quantitation-based proteomics analysis of ER-stressed rice (Oryza sativa) seeds. Unlike its homologs in yeast and mammals, which are located in the cytosol and respond to heat stress, OsFes1C is an ER membrane protein and responds to ER and salt stresses. OsFes1C interacts directly with OsBiP1 and the interaction is inhibited by ATP but promoted by ADP, suggesting that OsFes1C acts as a potential NEF of OsBiP1 in vivo. Overexpression or suppression of OsFes1C led to hypersensitivity to ER stress and affected the growth of rice. Furthermore, we established that OsFes1C directly interacts with a putative salt response protein and is involved in the salt response. Taken together, our study marks an important step toward elucidating the functional mechanisms of an identified ER stress response factor in rice. |
| تدمد: | 1532-2548 0032-0889 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bcdf6ae3eff2ce05f05ddff899ba561 https://doi.org/10.1093/plphys/kiab263 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....9bcdf6ae3eff2ce05f05ddff899ba561 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15322548 00320889 |
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