|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2009-4-13
|
|
pubmed:abstractText |
The anaphase-promoting complex or cyclosome (APC/C) is a ubiquitin ligase essential for the completion of mitosis in all eukaryotic cells. Substrates are recruited to the APC/C by activator proteins (Cdc20 or Cdh1), but it is not known where substrates are bound during catalysis. We explored this problem by analyzing mutations in the tetratricopeptide-repeat-containing APC/C subunits. We identified residues in Cdc23 and Cdc27 that are required for APC/C binding to Cdc20 and Cdh1 and for APC/C function in vivo. Mutation of these sites increased the rate of activator dissociation from the APC/C but did not affect reaction processivity, suggesting that the mutations have little effect on substrate dissociation from the active site. Further studies revealed that activator dissociation from the APC/C is inhibited by substrate, and that substrates are not bound solely to activator during catalysis but interact bivalently with an additional binding site on the APC/C core.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-10074450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-10786835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-11101887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-11553328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-11562348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-11566880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-12402045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-12574115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-12737816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-12956947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-14634663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-14659697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-14731401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-15166314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-15649358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-15916960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-15916961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16113654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16194281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16275331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16364911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16364912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16455800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16481473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16648845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-16896351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-17114580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-17493939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-17612486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-17632060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-17912263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-18082611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-18498748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-19026787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19362536-19394289
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1097-4164
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
10
|
|
pubmed:volume |
34
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
68-80
|
|
pubmed:dateRevised |
2011-6-2
|
|
pubmed:meshHeading |
pubmed-meshheading:19362536-Amino Acid Motifs,
pubmed-meshheading:19362536-Amino Acid Sequence,
pubmed-meshheading:19362536-Binding Sites,
pubmed-meshheading:19362536-Cell Cycle Proteins,
pubmed-meshheading:19362536-Enzyme Activation,
pubmed-meshheading:19362536-Models, Biological,
pubmed-meshheading:19362536-Molecular Sequence Data,
pubmed-meshheading:19362536-Mutation,
pubmed-meshheading:19362536-Protein Binding,
pubmed-meshheading:19362536-Saccharomyces cerevisiae,
pubmed-meshheading:19362536-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19362536-Sequence Analysis, Protein,
pubmed-meshheading:19362536-Ubiquitin-Protein Ligase Complexes
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
Analysis of activator-binding sites on the APC/C supports a cooperative substrate-binding mechanism.
|
|
pubmed:affiliation |
Department of Physiology, University of California, San Francisco, San Francisco, CA 94158, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|
