Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5353
pubmed:dateCreated
1998-3-5
pubmed:abstractText
The spindle checkpoint regulates the cell division cycle by keeping cells with defective spindles from leaving mitosis. In the two-hybrid system, three proteins that are components of the checkpoint, Mad1, Mad2, and Mad3, were shown to interact with Cdc20, a protein required for exit from mitosis. Mad2 and Mad3 coprecipitated with Cdc20 at all stages of the cell cycle. The binding of Mad2 depended on Mad1 and that of Mad3 on Mad1 and Mad2. Overexpression of Cdc20 allowed cells with a depolymerized spindle or damaged DNA to leave mitosis but did not overcome the arrest caused by unreplicated DNA. Mutants in Cdc20 that were resistant to the spindle checkpoint no longer bound Mad proteins, suggesting that Cdc20 is the target of the spindle checkpoint.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CDC20 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Cadherins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hct1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/MAD1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MAD1L1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/MAD2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1041-4
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:9461437-Amino Acid Sequence, pubmed-meshheading:9461437-Anaphase, pubmed-meshheading:9461437-Cadherins, pubmed-meshheading:9461437-Calcium-Binding Proteins, pubmed-meshheading:9461437-Carrier Proteins, pubmed-meshheading:9461437-Cell Cycle Proteins, pubmed-meshheading:9461437-DNA Damage, pubmed-meshheading:9461437-DNA Replication, pubmed-meshheading:9461437-Fungal Proteins, pubmed-meshheading:9461437-Ligases, pubmed-meshheading:9461437-Mitosis, pubmed-meshheading:9461437-Mitotic Spindle Apparatus, pubmed-meshheading:9461437-Molecular Sequence Data, pubmed-meshheading:9461437-Mutation, pubmed-meshheading:9461437-Nuclear Proteins, pubmed-meshheading:9461437-Phosphoproteins, pubmed-meshheading:9461437-Repressor Proteins, pubmed-meshheading:9461437-Saccharomyces cerevisiae, pubmed-meshheading:9461437-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9461437-Ubiquitin-Protein Ligase Complexes, pubmed-meshheading:9461437-Ubiquitin-Protein Ligases
pubmed:year
1998
pubmed:articleTitle
Budding yeast Cdc20: a target of the spindle checkpoint.
pubmed:affiliation
Department of Physiology, University of California at San Francisco, San Francisco, CA 94143-0444, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't