Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-4-2
pubmed:abstractText
Several subunits of the class III phosphatidylinositol-3-OH kinase (PI(3)K-III) complex are known as tumour suppressors. Here we uncover a function for this complex and its catalytic product phosphatidylinositol-3-phosphate (PtdIns(3)P) in cytokinesis. We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis. Translocation of FYVE-CENT and TTC19 from the centrosome to the midbody requires another FYVE-CENT-interacting protein, the microtubule motor KIF13A. Depletion of the VPS34 or Beclin 1 subunits of PI(3)K-III causes cytokinesis arrest and an increased number of binucleate and multinucleate cells, in a similar manner to the depletion of FYVE-CENT, KIF13A or TTC19. These results provide a mechanism for the translocation and docking of a cytokinesis regulatory machinery at the midbody.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins, http://linkedlifedata.com/resource/pubmed/chemical/BECN1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CHMP4B protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endosomal Sorting Complexes..., http://linkedlifedata.com/resource/pubmed/chemical/KIF13A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Kinesin, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol 3-phosphate, http://linkedlifedata.com/resource/pubmed/chemical/spastizin protein, human
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1476-4679
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
362-71
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:20208530-Animals, pubmed-meshheading:20208530-Apoptosis Regulatory Proteins, pubmed-meshheading:20208530-Biosensing Techniques, pubmed-meshheading:20208530-Carrier Proteins, pubmed-meshheading:20208530-Cell Cycle, pubmed-meshheading:20208530-Centrosome, pubmed-meshheading:20208530-Cytokinesis, pubmed-meshheading:20208530-Drosophila, pubmed-meshheading:20208530-Drosophila Proteins, pubmed-meshheading:20208530-Endosomal Sorting Complexes Required for Transport, pubmed-meshheading:20208530-HeLa Cells, pubmed-meshheading:20208530-Humans, pubmed-meshheading:20208530-Kinesin, pubmed-meshheading:20208530-Membrane Proteins, pubmed-meshheading:20208530-Mice, pubmed-meshheading:20208530-Microscopy, Fluorescence, pubmed-meshheading:20208530-Mitosis, pubmed-meshheading:20208530-Mitotic Spindle Apparatus, pubmed-meshheading:20208530-Mutation, pubmed-meshheading:20208530-Phosphatidylinositol 3-Kinases, pubmed-meshheading:20208530-Phosphatidylinositol Phosphates, pubmed-meshheading:20208530-Protein Binding, pubmed-meshheading:20208530-Protein Transport, pubmed-meshheading:20208530-RNA Interference, pubmed-meshheading:20208530-Recombinant Fusion Proteins, pubmed-meshheading:20208530-Signal Transduction, pubmed-meshheading:20208530-Transfection
pubmed:year
2010
pubmed:articleTitle
PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody.
pubmed:affiliation
Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Montebello, N-0310 Oslo, Norway.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't