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Yeast spindle pole bodies (SPBs) duplicate once per cell cycle by a conservative mechanism resulting in a pre-existing 'old' and a newly formed SPB. The two SPBs of yeast cells are functionally distinct. It is only the SPB that migrates into the daughter cell, the bud, which carries the Bfa1p-Bub2p GTPase-activating protein (GAP) complex, a component of the spindle positioning checkpoint. We investigated whether the functional difference of the two SPBs correlates with the time of their assembly. We describe that in unperturbed cells the 'old' SPB always migrates into the bud. However, Bfa1p localization is not determined by SPB inheritance. It is the differential interaction of cytoplasmic microtubules with the mother and bud cortex that directs the Bfa1p-Bub2p GAP to the bud-ward-localized SPB. In response to defects of cytoplasmic microtubules to interact with the cell cortex, the Bfa1p-Bub2p complex binds to both SPBs. This may provide a mechanism to delay cell cycle progression when cytoplasmic microtubules fail to orient the spindle. Thus, SPBs are able to sense cytoplasmic microtubule properties and regulate the Bfa1p-Bub2p GAP accordingly.

Original publication

DOI

10.1093/emboj/20.22.6359

Type

Journal article

Journal

EMBO J

Publication Date

15/11/2001

Volume

20

Pages

6359 - 6370

Keywords

Antineoplastic Agents, Cell Cycle Proteins, Cell Division, Cytoplasm, Cytoskeletal Proteins, Fluorescent Antibody Technique, Indirect, Fungal Proteins, GTPase-Activating Proteins, Genotype, Green Fluorescent Proteins, Luminescent Proteins, Microscopy, Confocal, Microscopy, Fluorescence, Microtubules, Models, Biological, Nocodazole, Phosphoproteins, Plasmids, Protein Binding, Saccharomyces cerevisiae Proteins, Saccharomycetales, Time Factors