Source:http://linkedlifedata.com/resource/pubmed/id/17488632
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2007-5-9
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pubmed:abstractText |
During cytokinesis, constriction of a cortical contractile ring generates a furrow that partitions one cell into two. The contractile ring contains three filament systems: actin, bipolar myosin II filaments, and septins, GTP-binding hetero-oligomers that polymerize to form a membrane-associated lattice. The contractile ring also contains a potential filament crosslinker, Anillin, that binds all three filament types. Here, we show that the contractile ring possesses an intrinsic symmetry-breaking mechanism that promotes asymmetric furrowing. Asymmetric ingression requires Anillin and the septins, which promote the coalescence of components on one side of the contractile ring, but is insensitive to a 10-fold reduction in myosin II levels. When asymmetry is disrupted, cytokinesis becomes sensitive to partial inhibition of contractility. Thus, asymmetric furrow ingression, a prevalent but previously unexplored feature of cell division in metazoans, is generated by the action of two conserved furrow components and serves a mechanical function that makes cytokinesis robust.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Contractile Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/anillin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1534-5807
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
827-35
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pubmed:meshHeading |
pubmed-meshheading:17488632-Animals,
pubmed-meshheading:17488632-Caenorhabditis elegans,
pubmed-meshheading:17488632-Caenorhabditis elegans Proteins,
pubmed-meshheading:17488632-Contractile Proteins,
pubmed-meshheading:17488632-Cytokinesis,
pubmed-meshheading:17488632-Drosophila melanogaster,
pubmed-meshheading:17488632-Embryo, Nonmammalian,
pubmed-meshheading:17488632-Myosin Type II,
pubmed-meshheading:17488632-Recombinant Fusion Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Anillin and the septins promote asymmetric ingression of the cytokinetic furrow.
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pubmed:affiliation |
Ludwig Institute for Cancer Research, Department of Cellular and Molecular Medicine (UCSD), CMM-East Rm. 3053, 9500 Gilman Drive, La Jolla, CA 92093, USA. amaddox@ucsd.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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