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Aurora kinases and protein phosphatase 1 mediate chromosome congression through regulation of CENP-E

聚焦生物添加于 2015-8-2 22:22 | 1762 次阅读 | 0 个评论

作者
Kim Y, Holland AJ, Lan W, Cleveland DW
摘要
Opposing roles of Aurora kinases and protein phosphatase 1 (PP1) during mitosis have long been suggested. Here, we demonstrate that Aurora kinases A and B phosphorylate a conserved residue on the kinetochore motor CENP-E. PP1 binds CENP-E via a motif overlapping this phosphorylation site and binding is disrupted by Aurora phosphorylation. Phosphorylation of CENP-E by the Auroras is enriched at spindle poles, disrupting binding of PP1 and reducing CENP-E\'s affinity for individual microtubules. This phosphorylation is required for CENP-E-mediated towing of initially polar chromosomes toward the cell center. Kinetochores on such chromosomes cannot make subsequent stable attachment to spindle microtubules when dephosphorylation of CENP-E or rebinding of PP1 to CENP-E is blocked. Thus, an Aurora/PP1 phosphorylation switch modulates CENP-E motor activity as an essential feature of chromosome congression from poles and localized PP1 delivery by CENP-E to the outer kinetochore is necessary for stable microtubule capture by those chromosomes.
详细资料
- 关键词: Amino Acid Sequence; Animals; Aurora Kinases; Chromosomal Proteins, Non-Histone/*metabolism; Chromosomes/*metabolism; HeLa Cells; Humans; Kinetochores/metabolism; Microtubules/metabolism; Molecular Sequence Data; Phosphorylation; Protein Phosphatase 1/*metabolism; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases/*metabolism; Sequence Alignment; Spindle Apparatus/metabolism; Xenopus laevis/*metabolism
- 文献种类:期刊
- 期刊名称: Cell
- 期刊缩写: Cell
- 期卷页: 2010年第142卷第3期 444-455页
- 地址: Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, CA 92093, USA
- ISBN: 0092-8674
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