pubmed-article:20377885 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20377885 | lifeskim:mentions | umls-concept:C0887872 | lld:lifeskim |
pubmed-article:20377885 | pubmed:dateCreated | 2010-5-12 | lld:pubmed |
pubmed-article:20377885 | pubmed:abstractText | One of the four principal categories of cell-cell junctions that hold together and shape distinct tissues and organs in vertebrates, adherens junctions (AJs) form cell-cell contacts that connect transmembrane proteins with cytoskeletal actin filaments to provide architectural strength, aid in morphogenesis, and help to maintain proper tissue homeostasis. The classical organization of AJs, consisting of transmembrane cadherins and cytoplasmically attached beta-catenins and alpha-catenins assembled together into a multiprotein complex, was once thought obligatory to craft a robust and stable connection to actin-based cytoskeletal elements, but this architecture has since been challenged and questioned to exist. In a stimulating paper published in a recent issue of BMC Biology, Millán et al. provide convincing evidence that in confluent vascular endothelial cells a novel dynamic vascular endothelial (VE)-cadherin-based AJ type exists that interacts with and physically connects prominent bundles of tension-mediating actin filaments, stress fibers, between neighboring cells. Stress fibers were known previously to link to integrin-based focal adhesion complexes but not to cell-cell adhesion mediating AJs. These new findings, together with previous results support the concept that different AJ subtypes, sharing the same transmembrane cadherin types, can assemble in various configurations to either increase barrier function and promote physical cell-cell adhesion, or to lessen cell-cell adhesion and promote cell separation and migration. | lld:pubmed |
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pubmed-article:20377885 | pubmed:language | eng | lld:pubmed |
pubmed-article:20377885 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20377885 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:20377885 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20377885 | pubmed:issn | 1741-7007 | lld:pubmed |
pubmed-article:20377885 | pubmed:author | pubmed-author:FalkMatthias... | lld:pubmed |
pubmed-article:20377885 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20377885 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:20377885 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20377885 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20377885 | pubmed:pagination | 34 | lld:pubmed |
pubmed-article:20377885 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
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pubmed-article:20377885 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20377885 | pubmed:articleTitle | Adherens junctions remain dynamic. | lld:pubmed |
pubmed-article:20377885 | pubmed:affiliation | Department of Biology, Lehigh University, Bethlehem, PA, USA. mfalk@lehigh.edu | lld:pubmed |
pubmed-article:20377885 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20377885 | pubmed:publicationType | Comment | lld:pubmed |
pubmed-article:20377885 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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