Plk1 phosphorylates CLIP-170 and regulates its binding to microtubules for chromosome alignment

Mai Kakeno, Kenji Matsuzawa, Toshinori Matsui, Hiroki Akita, Ikuko Sugiyama, Fumiyoshi Ishidate, Atsushi Nakano, Seiji Takashima, Hidemasa Goto, Masaki Inagaki, Kozo Kaibuchi, Takashi Watanabe

研究成果: ジャーナルへの寄稿学術論文査読

14 被引用数 (Scopus)

抄録

The microtubule (MT) cytoskeleton is essential for cellular morphogenesis, cell migration, and cell division. MT organization is primarily mediated by a variety of MT-associated proteins. Among these proteins, plus-end-tracking proteins (+TIPs) are evolutionarily conserved factors that selectively accumulate at growing MT plus ends. Cytoplasmic linker protein (CLIP)-170 is a +TIP that associates with diverse proteins to determine the behavior of MT ends and their linkage to intracellular structures, including mitotic chromosomes. However, how CLIP-170 activity is spatially and temporally controlled is largely unknown. Here, we show that phosphorylation at Ser312 in the third serine-rich region of CLIP-170 is increased during mitosis. Polo-like kinase 1 (Plk1) is responsible for this phosphorylation during the mitotic phase of dividing cells. In vitro analysis using a purified CLIP-170 N-terminal fragment showed that phosphorylation by Plk1 diminishes CLIP-170 binding to the MT ends and lattice without affecting binding to EB3. Furthermore, we demonstrate that during mitosis, stable kinetochore/MT attachment and subsequent chromosome alignment require CLIP-170 and a proper phosphorylation/dephosphorylation cycle at Ser312. We propose that CLIP-170 phosphorylation by Plk1 regulates proper chromosome alignment by modulating the interaction between CLIP-170 and MTs in mitotic cells and that CLIP-170 activity is stringently controlled by its phosphorylation state, which depends on the cellular context.

本文言語英語
ページ(範囲)45-59
ページ数15
ジャーナルCell structure and function
39
1
DOI
出版ステータス出版済み - 2014
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生理学
  • 分子生物学
  • 細胞生物学

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