GRASP65 controls Golgi position and structure during G2/M transition by regulating the stability of microtubules
| العنوان: | GRASP65 controls Golgi position and structure during G2/M transition by regulating the stability of microtubules |
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| المؤلفون: | Roberta Crispino, Antonino Colanzi, Inmaculada Ayala |
| المصدر: | Traffic (Online) (2019): 785–802. doi:10.1111/tra.12682 info:cnr-pdr/source/autori:Ayala I, Crispino R, Colanzi A/titolo:GRASP65 controls Golgi position and structure during G2%2FM transition by regulating the stability of microtubules./doi:10.1111%2Ftra.12682/rivista:Traffic (Online)/anno:2019/pagina_da:785/pagina_a:802/intervallo_pagine:785–802/volume |
| بيانات النشر: | Wiley, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | G2 Phase, Cell division, MAP Kinase Kinase 4, Golgi Apparatus, Cell cycle Tubulin, Biology, Microtubules, Biochemistry, 03 medical and health sciences, symbols.namesake, 0302 clinical medicine, Tubulin, Structural Biology, Microtubule, Golgi, Genetics, Humans, Molecular Biology, Mitosis, 030304 developmental biology, Microtubule nucleation, Mitogen-Activated Protein Kinase 1, 0303 health sciences, Mitogen-Activated Protein Kinase 3, Golgi Matrix Proteins, Cell Biology, Cell cycle, Golgi apparatus, Cell biology, Acetylation, Centrosome, symbols, Cell Division, 030217 neurology & neurosurgery, HeLa Cells |
| الوصف: | The mammalian Golgi apparatus is organized in the form of a ribbon-like structure positioned near the centrosome. Despite its multimodular organization, the Golgi complex is characterized by a prominent structural plasticity, which is crucial during essential physiological processes, such as the G2 phase of the cell cycle, during which the Golgi ribbon must be "unlinked" into isolated stacks to allow progression into mitosis. Here we show that the Golgi-associated protein GRASP65, which is well known for its role in Golgi stacking and ribbon formation, is also required for the organization of the microtubule cytoskeleton. GRASP65 is not involved in microtubule nucleation or anchoring. Instead, it is required for the stabilization of newly nucleated microtubules, leading to their acetylation and clustering of Golgi stacks. Ribbon formation and microtubule stabilization are both regulated by JNK/ERK-mediated phosphorylation of S274 of GRASP65, suggesting that this protein can coordinate the Golgi structure with microtubule organization. In agreement with and important role, tubulin acetylation is strongly reduced during the G2 phase of the cell cycle, allowing the separation of the Golgi stacks. Thus, our data reveal a fundamental role of GRASP65 in the integration of different stimuli to modulate Golgi structure and microtubule organization during cell division. This article is protected by copyright. All rights reserved. |
| تدمد: | 1600-0854 1398-9219 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6ff4865e0d95efd2e0c249b12c4afdeTest https://doi.org/10.1111/tra.12682Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e6ff4865e0d95efd2e0c249b12c4afde |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16000854 13989219 |
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