Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-8-22
pubmed:abstractText
Three lines of investigation have suggested that interactions between Survivin and the chromosomal passenger proteins INCENP and Aurora-B kinase may be important for mitotic progression. First, interference with the function of Survivin/BIR1, INCENP, or Aurora-B kinase leads to similar defects in mitosis and cytokinesis [1-7] (see [8] for review). Second, INCENP and Aurora-B exist in a complex in Xenopus eggs [9] and in mammalian cultured cells [7]. Third, interference with Survivin or INCENP function causes Aurora-B kinase to be mislocalized in mitosis in both C. elegans and vertebrates [5, 7, 9]. Here, we provide evidence that Survivin, Aurora-B, and INCENP interact physically and functionally. Direct visualization of Survivin-GFP in mitotic cells reveals that it localizes identically to INCENP and Aurora-B. Survivin binds directly to both Aurora-B and INCENP in yeast two-hybrid and in vitro pull-down assays. The in vitro interaction between Survivin and Aurora-B is extraordinarily stable in that it resists 3 M NaCl. Finally, Survivin and INCENP interact functionally in vivo; in cells in which INCENP localization is disrupted, Survivin adheres to the chromosomes and no longer concentrates at the centromeres or transfers to the anaphase spindle midzone. Our data provide the first biochemical evidence that Survivin can interact directly with members of the chromosomal passenger complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
886-90
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11516652-Anaphase, pubmed-meshheading:11516652-Animals, pubmed-meshheading:11516652-Carrier Proteins, pubmed-meshheading:11516652-Cell Compartmentation, pubmed-meshheading:11516652-Centromere, pubmed-meshheading:11516652-Chickens, pubmed-meshheading:11516652-Chromosomal Proteins, Non-Histone, pubmed-meshheading:11516652-HeLa Cells, pubmed-meshheading:11516652-Humans, pubmed-meshheading:11516652-Inhibitor of Apoptosis Proteins, pubmed-meshheading:11516652-Microtubule-Associated Proteins, pubmed-meshheading:11516652-Mitotic Spindle Apparatus, pubmed-meshheading:11516652-Mutation, pubmed-meshheading:11516652-Neoplasm Proteins, pubmed-meshheading:11516652-Protein Binding, pubmed-meshheading:11516652-Protein Transport, pubmed-meshheading:11516652-Protein-Serine-Threonine Kinases, pubmed-meshheading:11516652-Tumor Cells, Cultured, pubmed-meshheading:11516652-Two-Hybrid System Techniques
pubmed:year
2001
pubmed:articleTitle
INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis.
pubmed:affiliation
Chromosome Structure Group, Institute of Cell and Molecular Biology, Swann Building, University of Edinburgh, King's Buildings, Mayfield Road, EH9 3JR, Edinburgh, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't