Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-12-16
pubmed:abstractText
Human Aurora/Ipl1-related kinase 2 (Aurora-B) is a key regulator of mitosis. Here human proteasome alpha-subunit C8 (HC8) was identified to interact with the Aurora-B by yeast two-hybrid screen. This finding was confirmed by GST pull-down assays and immunoprecipitation experiments. The Aurora-B protein level increased in HeLa cells cultured with proteasome inhibitor ALLN. Our data suggest that Aurora-B might undergo degradation by binding to HC8 in a proteasome-dependent manner during mitosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-62
pubmed:dateRevised
2011-7-11
pubmed:meshHeading
pubmed-meshheading:14674694-Cell Cycle, pubmed-meshheading:14674694-Cysteine Endopeptidases, pubmed-meshheading:14674694-DNA, Complementary, pubmed-meshheading:14674694-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:14674694-Glutathione Transferase, pubmed-meshheading:14674694-HeLa Cells, pubmed-meshheading:14674694-Humans, pubmed-meshheading:14674694-Immunoblotting, pubmed-meshheading:14674694-Mitosis, pubmed-meshheading:14674694-Multienzyme Complexes, pubmed-meshheading:14674694-Plasmids, pubmed-meshheading:14674694-Precipitin Tests, pubmed-meshheading:14674694-Proteasome Endopeptidase Complex, pubmed-meshheading:14674694-Protein Binding, pubmed-meshheading:14674694-Protein Biosynthesis, pubmed-meshheading:14674694-Protein-Serine-Threonine Kinases, pubmed-meshheading:14674694-Two-Hybrid System Techniques
pubmed:year
2003
pubmed:articleTitle
Human aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner.
pubmed:affiliation
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't