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rdf:type |
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lifeskim:mentions |
umls-concept:C0007709,
umls-concept:C0019647,
umls-concept:C0077678,
umls-concept:C0205419,
umls-concept:C0475264,
umls-concept:C0574895,
umls-concept:C0599894,
umls-concept:C1292733,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
2010-11-12
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pubmed:abstractText |
Proper centromere function is critical to maintain genomic stability and to prevent aneuploidy, a hallmark of tumors and birth defects. A conserved feature of all eukaryotic centromeres is an essential histone H3 variant called CENP-A that requires a centromere targeting domain (CATD) for its localization. Although proteolysis prevents CENP-A from mislocalizing to euchromatin, regulatory factors have not been identified. Here, we identify an E3 ubiquitin ligase called Psh1 that leads to the degradation of Cse4, the budding yeast CENP-A homolog. Cse4 overexpression is toxic to psh1? cells and results in euchromatic localization. Strikingly, the Cse4 CATD is a key regulator of its stability and helps Psh1 discriminate Cse4 from histone H3. Taken together, we propose that the CATD has a previously unknown role in maintaining the exclusive localization of Cse4 by preventing its mislocalization to euchromatin via Psh1-mediated degradation.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CSE4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Euchromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Psh1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1097-4164
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
455-64
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
pubmed-meshheading:21070971-Amino Acid Sequence,
pubmed-meshheading:21070971-Centromere,
pubmed-meshheading:21070971-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:21070971-DNA-Binding Proteins,
pubmed-meshheading:21070971-Euchromatin,
pubmed-meshheading:21070971-Histones,
pubmed-meshheading:21070971-Molecular Sequence Data,
pubmed-meshheading:21070971-Mutation,
pubmed-meshheading:21070971-Peptide Elongation Factors,
pubmed-meshheading:21070971-Protein Binding,
pubmed-meshheading:21070971-Protein Isoforms,
pubmed-meshheading:21070971-Protein Processing, Post-Translational,
pubmed-meshheading:21070971-Protein Stability,
pubmed-meshheading:21070971-Protein Structure, Tertiary,
pubmed-meshheading:21070971-Protein Transport,
pubmed-meshheading:21070971-Saccharomyces cerevisiae,
pubmed-meshheading:21070971-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:21070971-Ubiquitin-Protein Ligases,
pubmed-meshheading:21070971-Ubiquitination
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pubmed:year |
2010
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pubmed:articleTitle |
An E3 ubiquitin ligase prevents ectopic localization of the centromeric histone H3 variant via the centromere targeting domain.
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pubmed:affiliation |
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N., P.O. Box 19024, Seattle, WA 98109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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