Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae

Chong J. Park, Sukgil Song, Thomas H. Giddings, Hyeon Su Ro, Krisada Sakchaisri, Jung Eun Park, Yeon Sun Seong, Mark Winey, Kyung S. Lee

Research output: Contribution to journalArticle

13 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1711-1723
Number of pages13
JournalMolecular Biology of the Cell
Volume15
Issue number4
DOIs
StatePublished - Apr 1 2004
Externally publishedYes

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Spindle Pole Bodies
Saccharomyces cerevisiae
Saccharomycetales
Fungal Proteins
Neck
Phosphotransferases

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Park, C. J., Song, S., Giddings, T. H., Ro, H. S., Sakchaisri, K., Park, J. E., ... Lee, K. S. (2004). Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae. Molecular Biology of the Cell, 15(4), 1711-1723. https://doi.org/10.1091/mbc.E03-07-0461

Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae. / Park, Chong J.; Song, Sukgil; Giddings, Thomas H.; Ro, Hyeon Su; Sakchaisri, Krisada; Park, Jung Eun; Seong, Yeon Sun; Winey, Mark; Lee, Kyung S.

In: Molecular Biology of the Cell, Vol. 15, No. 4, 01.04.2004, p. 1711-1723.

Research output: Contribution to journalArticle

Park, CJ, Song, S, Giddings, TH, Ro, HS, Sakchaisri, K, Park, JE, Seong, YS, Winey, M & Lee, KS 2004, 'Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae', Molecular Biology of the Cell, vol. 15, no. 4, pp. 1711-1723. https://doi.org/10.1091/mbc.E03-07-0461
Park, Chong J. ; Song, Sukgil ; Giddings, Thomas H. ; Ro, Hyeon Su ; Sakchaisri, Krisada ; Park, Jung Eun ; Seong, Yeon Sun ; Winey, Mark ; Lee, Kyung S. / Requirement for Bbp1p in the Proper Mitotic Functions of Cdc5p in Saccharomyces cerevisiae. In: Molecular Biology of the Cell. 2004 ; Vol. 15, No. 4. pp. 1711-1723.
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AU - Ro, Hyeon Su

AU - Sakchaisri, Krisada

AU - Park, Jung Eun

AU - Seong, Yeon Sun

AU - Winey, Mark

AU - Lee, Kyung S.

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AB - 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.

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