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

Chii Shyang Fong, Masamitsu Sato, Takashi Toda*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)120-130
Number of pages11
JournalEMBO Journal
Issue number1
Publication statusPublished - 2010 Jan 6
Externally publishedYes


  • Centrosome
  • Nuclear envelope
  • Polo kinase
  • SPB
  • γ-tubulin complex

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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