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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2005-12-5
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pubmed:abstractText |
Epithelial cell-cell junctions, organized by adhesion proteins and the underlying actin cytoskeleton, are considered to be stable structures maintaining the structural integrity of tissues. Contrary to the idea that alpha-catenin links the adhesion protein E-cadherin through beta-catenin to the actin cytoskeleton, in the accompanying paper we report that alpha-catenin does not bind simultaneously to both E-cadherin-beta-catenin and actin filaments. Here we demonstrate that alpha-catenin exists as a monomer or a homodimer with different binding properties. Monomeric alpha-catenin binds more strongly to E-cadherin-beta-catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that alpha-catenin is an allosteric protein. Significantly, alpha-catenin directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments. These results indicate a new role for alpha-catenin in local regulation of actin assembly and organization at sites of cadherin-mediated cell-cell adhesion.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
903-15
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16325583-Actin-Related Protein 2-3 Complex,
pubmed-meshheading:16325583-Actins,
pubmed-meshheading:16325583-Animals,
pubmed-meshheading:16325583-Cadherins,
pubmed-meshheading:16325583-Cell Adhesion,
pubmed-meshheading:16325583-Cell Membrane,
pubmed-meshheading:16325583-Cytoskeleton,
pubmed-meshheading:16325583-Dimerization,
pubmed-meshheading:16325583-Mice,
pubmed-meshheading:16325583-Models, Molecular,
pubmed-meshheading:16325583-Multiprotein Complexes,
pubmed-meshheading:16325583-Protein Binding,
pubmed-meshheading:16325583-Protein Conformation,
pubmed-meshheading:16325583-Protein Subunits,
pubmed-meshheading:16325583-Recombinant Proteins,
pubmed-meshheading:16325583-Vinculin,
pubmed-meshheading:16325583-alpha Catenin,
pubmed-meshheading:16325583-beta Catenin
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pubmed:year |
2005
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pubmed:articleTitle |
Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly.
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pubmed:affiliation |
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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