Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-9-5
pubmed:abstractText
Cdc20 is a substrate adaptor and activator of the anaphase-promoting complex/cyclosome (APC/C), the E3 ubiquitin ligase whose activity is required for anaphase onset and exit from mitosis. A green fluorescent protein derivative, Cdc20-GFP, bound to centrosomes throughout the cell cycle and to kinetochores from late prophase to late telophase. We mapped distinct domains of Cdc20 that are required for association with kinetochores and centrosomes. FRAP measurements revealed extremely rapid dynamics at the kinetochores (t1/2 = 5.1 s) and spindle poles (t1/2 = 4.7 s). This rapid turnover is independent of microtubules. Rapid transit of Cdc20 through kinetochores may ensure that spindle checkpoint signaling at unattached/relaxed kinetochores can continuously inhibit APC/CCdc20 targeting of anaphase inhibitors (securins) throughout the cell until all the chromosomes are properly attached to the mitotic spindle.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-10477750, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-10619133, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-10995431, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11438673, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11535616, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11553328, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11676939, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11702782, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11726501, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11747833, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11756470, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-11907259, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-12006501, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-8824188, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9353311, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9356466, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9628895, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9637688, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9660858, http://linkedlifedata.com/resource/pubmed/commentcorrection/12196507-9786942
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bub1 spindle checkpoint protein, http://linkedlifedata.com/resource/pubmed/chemical/CDC20 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/MAD2L1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, 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/anaphase-promoting complex
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
158
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
841-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12196507-Animals, pubmed-meshheading:12196507-Calcium-Binding Proteins, pubmed-meshheading:12196507-Cell Cycle Proteins, pubmed-meshheading:12196507-Centrosome, pubmed-meshheading:12196507-Fluorescence Recovery After Photobleaching, pubmed-meshheading:12196507-HeLa Cells, pubmed-meshheading:12196507-Humans, pubmed-meshheading:12196507-Kinetochores, pubmed-meshheading:12196507-LLC-PK1 Cells, pubmed-meshheading:12196507-Ligases, pubmed-meshheading:12196507-Microscopy, Fluorescence, pubmed-meshheading:12196507-Microtubules, pubmed-meshheading:12196507-Mitosis, pubmed-meshheading:12196507-Models, Biological, pubmed-meshheading:12196507-Protein Kinases, pubmed-meshheading:12196507-Protein Structure, Tertiary, pubmed-meshheading:12196507-Protein-Serine-Threonine Kinases, pubmed-meshheading:12196507-Repressor Proteins, pubmed-meshheading:12196507-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12196507-Time Factors, pubmed-meshheading:12196507-Ubiquitin-Protein Ligase Complexes
pubmed:year
2002
pubmed:articleTitle
Rapid microtubule-independent dynamics of Cdc20 at kinetochores and centrosomes in mammalian cells.
pubmed:affiliation
University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. marko-kallio@ouhsc.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't