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Title 

Requirement for Bbp1p in the proper mitotic functions of Cdc5p in Saccharomyces cerevisiae

Authors 

C J ParkS G SongT H GiddingsHyeon Su RoK SakchaisriJ E ParkY S SeongM WineyK S Lee

Publisher 

American Society for Cell Biology

Issue Date 

2004

Citation 

Molecular Biology of the Cell, vol. 15, no. 4, pp. 1711-1723

Keywords 

protein Bbp1pprotein cdc5pprotein functionsaccharomyces cerevisiaemitotic spindle apparatussaccharomyces cerevisiae proteinssaccharomyces

Abstract 

The polo-box domain of the budding yeast polo kinase Cdc5p plays an essential role for targeting the catalytic activity of Cdc5p to spindle pole bodies (SPBs) and cytokinetic neck-filaments. Here, we report the isolation of Bbp1p as a polo-box interacting protein by a yeast two-hybrid screen. Bbp1p localizes to the periphery of the central plaque of the SPB and plays an important role in SPB duplication. Similarly, Cdc5p localized to the cytoplasmic periphery of the SPB. In vitro binding studies showed that Cdc5p interacted with the N-terminal domain of Bbp1p (Bbp1pΔC), but apparently not with Mps2p, a component shown to form a stable complex with Bbp1p. In addition, Bbp1p, but likely not Mps2p, was required for proper localization of Cdc5p to the SPB. The C-terminal coiled-coil domain of Bbp1p (Bbp1p 243-385), which is crucial for both the homodimerization and the SPB localization, could target the localization-defective Cdc5pΔC to the SPB and induce the release of Cdc14p from the nucleolus. Consistent with this observation, expression of CDC5ΔC-BBP1243-385 under CDC5 promoter control partially complemented the cdc5Δ defect. These data suggest that Bbp1pΔC interacts with the polo-box domain of Cdc5p, and this interaction is critical for the subcellular localization and mitotic functions of Cdc5p.

ISSN 

1059-1524

Link 

http://dx.doi.org/10.1091/mbc.E03-07-0461

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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