Fission yeast Pcp1 links polo kinase-mediated mitotic entry to c-tubulin-dependent spindle formation

Chii Shyang Fong, Masamitsu Sato, Takashi Toda*

*この研究の対応する著者

研究成果: Article査読

40 被引用数 (Scopus)

抄録

The centrosomal pericentrin-related proteins play pivotal roles in various aspects of cell division; however their underlying mechanisms remain largely elusive. Here we show that fission-yeast pericentrin-like Pcp1 regulates multiple functions of the spindle pole body (SPB) through recruiting two critical factors, the c-tubulin complex (c-TuC) and polo kinase (Plo1). We isolated two pcp1 mutants (pcp1-15 and pcp1-18) that display similar abnormal spindles, but with remarkably different molecular defects. Both mutants exhibit defective monopolar spindle microtubules that emanate from the mother SPB. However, while pcp1-15 fails to localise the c-TuC to the mitotic SPB, pcp1-18 is specifically defective in recruiting Plo1. Consistently Pcp1 forms a complex with both c-TuC and Plo1 in the cell. pcp1-18 is further defective in the mitoticspecific reorganisation of the nuclear envelope (NE), leading to impairment of SPB insertion into the NE. Moreover pcp1-18, but not pcp1-15, is rescued by overproducing nuclear pore components or advancing mitotic onset. The central role for Pcp1 in orchestrating these processes provides mechanistic insight into how the centrosome regulates multiple cellular pathways.

本文言語English
ページ(範囲)120-130
ページ数11
ジャーナルEMBO Journal
29
1
DOI
出版ステータスPublished - 2010 1月 6
外部発表はい

ASJC Scopus subject areas

  • 神経科学(全般)
  • 分子生物学
  • 生化学、遺伝学、分子生物学(全般)
  • 免疫学および微生物学(全般)

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