Abstract
Phosphorylation of the Ndc80 kinetochore protein by the Ipl1/Aurora B kinase reduces its microtubule binding activity in vitro. We found that kinetochore-bound Ndc80 is phosphorylated on Ipl1 sites in vivo, but this phosphorylation is not essential. Instead, we show that additional Ipl1 targets contribute to segregation and the spindle checkpoint.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aurora Kinases
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Intracellular Signaling Peptides and Proteins / metabolism*
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Kinetochores / chemistry
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Kinetochores / metabolism*
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Microtubules / metabolism
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Mutation
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Phosphorylation
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Protein Serine-Threonine Kinases / metabolism*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Intracellular Signaling Peptides and Proteins
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NDC80 protein, S cerevisiae
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Nuclear Proteins
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Saccharomyces cerevisiae Proteins
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Aurora Kinases
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IPL1 protein, S cerevisiae
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Protein Serine-Threonine Kinases