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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1987-12-30
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pubmed:abstractText |
Adhesion plaques, specialized regions of the plasma membrane where a cell contacts its substratum, are dynamic structures. However, little is known about how the protein-protein interactions that occur at adhesion plaques are controlled. One mechanism by which a cell might modulate its associations with the substratum is by selective, regulated proteolysis of an adhesion plaque component. Here we show that the catalytic subunit of the calcium-dependent protease type II (CDP-II) is localized in adhesion plaques of several cell types (BS-C-1, EBTr, and MDBK). We have compared the susceptibility of the adhesion plaque constituents vinculin, talin, and alpha-actinin to calcium-dependent proteolysis in vitro and have found talin to be the preferred substrate for CDP-II. The colocalization of a calcium-requiring proteolytic enzyme and talin in adhesion plaques raises the possibility that calcium-dependent proteolytic activity provides a mechanism for regulating some aspect of adhesion plaque physiology and function via cleavage of talin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actinin,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Talin,
http://linkedlifedata.com/resource/pubmed/chemical/Vinculin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
|
pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-77
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2824061-Actinin,
pubmed-meshheading:2824061-Animals,
pubmed-meshheading:2824061-Antigens, Surface,
pubmed-meshheading:2824061-Calpain,
pubmed-meshheading:2824061-Cattle,
pubmed-meshheading:2824061-Cell Adhesion,
pubmed-meshheading:2824061-Cell Adhesion Molecules,
pubmed-meshheading:2824061-Cell Line,
pubmed-meshheading:2824061-Cercopithecus aethiops,
pubmed-meshheading:2824061-Cytoskeletal Proteins,
pubmed-meshheading:2824061-Kidney,
pubmed-meshheading:2824061-Muscle Proteins,
pubmed-meshheading:2824061-Talin,
pubmed-meshheading:2824061-Vinculin
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pubmed:year |
1987
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pubmed:articleTitle |
Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion.
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pubmed:affiliation |
Department of Biology, University of Utah, Salt Lake City 84112.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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