The Role of GRASP55 in Golgi Fragmentation and Entry of Cells into Mitosis
| العنوان: | The Role of GRASP55 in Golgi Fragmentation and Entry of Cells into Mitosis |
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| المؤلفون: | Carine Bossard, Roman S. Polishchuk, Matt Kinseth, Vivek Malhotra, Timo Zimmerman, David W. Rose, John R. Yates, Juan M. Duran, Christine C. Wu |
| المصدر: | Molecular Biology of the Cell. 19:2579-2587 |
| بيانات النشر: | American Society for Cell Biology (ASCB), 2008. |
| سنة النشر: | 2008 |
| مصطلحات موضوعية: | Cell Extracts, Molecular Sequence Data, Cell, Golgi Apparatus, Mitosis, Golgi reassembly, Biology, Peptide Mapping, Cell Line, symbols.namesake, Antibody Specificity, medicine, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Phosphorylation, RNA, Small Interfering, Fragmentation (cell biology), Molecular Biology, Golgi organization, Golgi Matrix Proteins, Membrane Proteins, Articles, Cell Biology, Golgi apparatus, Phosphoproteins, Protein Structure, Tertiary, Rats, Cell biology, medicine.anatomical_structure, Cell culture, symbols |
| الوصف: | GRASP55 is a Golgi-associated protein, but its function at the Golgi remains unclear. Addition of full-length GRASP55, GRASP55-specific peptides, or an anti-GRASP55 antibody inhibited Golgi fragmentation by mitotic extracts in vitro, and entry of cells into mitosis. Phospho-peptide mapping of full-length GRASP55 revealed that threonine 225 and 249 were mitotically phosphorylated. Wild-type peptides containing T225 and T249 inhibited Golgi fragmentation and entry of cells into mitosis. Mutant peptides containing T225E and T249E, in contrast, did not affect Golgi fragmentation and entry into mitosis. These findings reveal a role of GRASP55 in events leading to Golgi fragmentation and the subsequent entry of cell into mitosis. Surprisingly, however, under our experimental conditions, >85% knockdown of GRASP55 did not affect the overall organization of Golgi organization in terms of cisternal stacking and lateral connections between stacks. Based on our findings we suggest that phosphorylation of GRASP55 at T225/T249 releases a bound component, which is phosphorylated and necessary for Golgi fragmentation. Thus, GRASP55 has no role in the organization of Golgi membranes per se, but it controls their fragmentation by regulating the release of a partner, which requires a G2-specific phosphorylation at T225/T249. |
| تدمد: | 1939-4586 1059-1524 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbb0f5509c06777cfab5efcf0a08b852Test https://doi.org/10.1091/mbc.e07-10-0998Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....fbb0f5509c06777cfab5efcf0a08b852 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19394586 10591524 |
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