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PMID: 17504936 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Ipl1p-dependent phosphorylation of Mad3p is required for the spindle checkpoint response to lack of tension at kinetochores.

Genes & development ·Vol. 21 ·No. 10 ·2007-05-15 ·Pages 1163-8

King EM, Rachidi N, Morrice N, Hardwick KG, Stark MJ

Abstract

The spindle checkpoint delays anaphase onset until all chromosomes are correctly attached to microtubules. Ipl1 protein kinase (Aurora B) is required to correct inappropriate kinetochore-microtubule attachments and for the response to lack of tension between sister kinetochores. Here we identify residues in the checkpoint protein Mad3p that are phosphorylated by Ipl1p. When phosphorylation of Mad3p at two sites is prevented, the cell's response to reduced kinetochore tension is dramatically curtailed. Our data provide strong evidence for a distinct checkpoint pathway responding to lack of sister kinetochore tension, in which Ipl1p-dependent phosphorylation of Mad3p is a key step.

MeSH Terms
Aurora Kinases Blotting, Western Cell Cycle Proteins/metabolism Electrophoresis, Polyacrylamide Gel Genes, cdc/physiology Immunohistochemistry Kinetochores/metabolism Nuclear Proteins/metabolism Protein Serine-Threonine Kinases/metabolism Saccharomyces cerevisiae Proteins/metabolism Spindle Apparatus/metabolism Yeasts
Chemicals
Cell Cycle Proteins MAD3 protein, S cerevisiae Nuclear Proteins Saccharomyces cerevisiae Proteins Aurora Kinases Protein Serine-Threonine Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
King Emma M J
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.
Rachidi Najma
Morrice Nick
Hardwick Kevin G
Stark Michael J R
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31 references, click to expand
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Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
Published
2007-05-15
Pages
1163-8
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC1865488
Subset
IM
Grants
Wellcome Trust · 067210 · United Kingdom
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