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Fission yeast Pcp1 links polo kinase‐mediated mitotic entry to γ‐tubulin‐dependent spindle formation
Author(s) -
Fong Chii Shyang,
Sato Masamitsu,
Toda Takashi
Publication year - 2010
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.331
Subject(s) - spindle pole body , centrosome , microbiology and biotechnology , biology , mitosis , polo like kinase , spindle apparatus , microtubule , multipolar spindles , microtubule organizing center , tubulin , microtubule nucleation , cell division , plk1 , cell cycle , genetics , cell
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 γ‐tubulin complex (γ‐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 γ‐TuC to the mitotic SPB, pcp1‐18 is specifically defective in recruiting Plo1. Consistently Pcp1 forms a complex with both γ‐TuC and Plo1 in the cell. pcp1‐18 is further defective in the mitotic‐specific 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.