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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45552

Title: Phosphorylation of NuSAP by Cdk1 regulates its interaction with microtubules in mitosis.
Authors: Han-Yi Chou;Ting-Huang Wang;Sheng-Chung Lee;Pang-Hung Hsu;Ming-Daw Tsai;Chih-Ling Chang;Yung-Ming Jeng
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2011
Issue Date: 2018-03-26T06:30:12Z
Publisher: Cell Cycle
Abstract: Abstract: Cell division in eukaryotes depends on a fine control of the dynamic changes of microtubules. Nucleolar and spindle-associated protein (NuSAP) is a microtubule-binding and -bundling protein essential for the integrity of the anaphase spindle and cell division. NuSAP contains two consensus cdk phosphorylation sites in its microtubule-binding domain. Here we show NuSAP is phosphorylated by cdk1 in early mitosis. This phosphorylation inhibits the binding of NuSAP to microtubules. During metaphase-to anaphase transition, NuSAP is dephosphorylated to promote spindle midzone formation and cell cycle progression. Expression of cdk1 phosphorylation-null mutant causes extensive bundling of microtubules in the prometaphase spindle. Our results suggest that phosphorylation and dephosphorylation of NuSAP during progression of mitosis regulate spindle organization through modulation of the dynamics of microtubules.
Relation: 10(23)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45552
Appears in Collections:[生命科學系] 期刊論文

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