Structure and functions of the chaperone-like p97/CDC48 in plants
| العنوان: | Structure and functions of the chaperone-like p97/CDC48 in plants |
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| المؤلفون: | Hervé Bègue, David Wendehenne, Cécile Blanchard, Claire Rosnoblet, Sylvain Jeandroz |
| المساهمون: | Agroécologie [Dijon], Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC), La Region de Bourgogne [PARI AGREE project], Université de Bourgogne (UB)-Institut National de la Recherche Agronomique (INRA)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Institut National de la Recherche Agronomique ( INRA ) -Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté ( UBFC ) |
| المصدر: | Biochimica et Biophysica Acta (BBA)-General Subjects Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2017, 1861 (1), pp.3053-3060. ⟨10.1016/j.bbagen.2016.10.001⟩ BBA-General Subjects BBA-General Subjects, Elsevier, 2017, 1861 (1), pp.3053-3060. 〈10.1016/j.bbagen.2016.10.001〉 |
| بيانات النشر: | HAL CCSD, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Protein turnover, [SDV]Life Sciences [q-bio], Biophysics, Plant Immunity, Cell Cycle Proteins, Endoplasmic-reticulum-associated protein degradation, Biochemistry, p97/CDC48/VCP, Evolution, Molecular, 03 medical and health sciences, Structure-Activity Relationship, Valosin Containing Protein, Molecular Biology, Ultrabithorax, Adenosine Triphosphatases, biology, [ SDV ] Life Sciences [q-bio], Autophagy, Immunity, Cell cycle, Plants, Cell biology, 030104 developmental biology, Chaperone (protein), biology.protein, Protein quality, Molecular Chaperones |
| الوصف: | Background The chaperone-like p97 is a member of the AAA + ATPase enzyme family that contributes to numerous cellular activities. P97 has been broadly studied in mammals (VCP/p97) and yeasts (CDC48: Cell Division Cycle 48/p97) and numerous investigations highlighted that this protein is post-translationally regulated, is structured in homohexamer and interacts with partners and cofactors that direct it to distinct cellular signalization pathway including protein quality control and degradation, cell cycle regulation, genome stability, vesicular trafficking, autophagy and immunity. Scope of review p97 is also conserved in plants (CDC48) but its functions are less understood. In the present review we intended to present the state of the art of the structure, regulation and functions of CDC48 in plants. Major conclusions Evidence accumulated underline that CDC48 plays a crucial role in development, cell cycle regulation and protein turnover in plants. Furthermore, its involvement in plant immunity has recently emerged and first interacting partners have been identified, shedding light on its putative cellular activities. General significance Identification of emerging functions of CDC48 in plants opens new roads of research in immunity and provides new insights into the mechanisms of protein quality control. |
| اللغة: | English |
| تدمد: | 0304-4165 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58f4c429bf2b26d972bf6e2175db94beTest https://hal.archives-ouvertes.fr/hal-01605686Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....58f4c429bf2b26d972bf6e2175db94be |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 03044165 |
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