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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1994-11-29
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pubmed:abstractText |
The isolated intestinal microvillus cytoskeleton (core) consists of four major proteins: actin, villin, fimbrin and brush border myosin-I. These proteins can assemble in vitro into structures resembling native microvillus cores. Of these components, villin and brush border myosin-I show tissue-specific expression, so they may be involved in the morphogenesis of intestinal microvilli. When introduced into cultured cells that normally lack the protein, villin induces a reorganization of the actin filaments to generate large surface microvilli. Here we examine the consequences of microinjecting brush border myosin-I either alone or together with villin into cultured fibroblasts. Injection of brush border myosin-I has no discernible effect on the overall morphology of the cells, but does become localized to either normal or villin-induced microvilli and other surface structures containing an actin cytoskeleton. Since some endogenous myosin-Is have been found associated with cytoplasmic vesicles, these results show that brush border myosin-I has a domain that specifically targets it to the plasma membrane in both intestinal and cultured cell systems. Ultrastructural examination of microvilli on control cultured cells revealed that they contain a far more highly ordered bundle of microfilaments than had been previously appreciated. The actin filaments in microvilli of villin-injected cells appeared to be more tightly cross-linked when examined by thin-section electron microscopy. In intestinal microvilli, the core bundle is separated from the plasma membrane by about 30 nm due to the presence of brush border myosin-I.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/villin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
107 ( Pt 6)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1623-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7962202-3T3 Cells,
pubmed-meshheading:7962202-Actins,
pubmed-meshheading:7962202-Animals,
pubmed-meshheading:7962202-Carrier Proteins,
pubmed-meshheading:7962202-Cells, Cultured,
pubmed-meshheading:7962202-Cytoskeleton,
pubmed-meshheading:7962202-Fluorescent Antibody Technique,
pubmed-meshheading:7962202-Intestinal Mucosa,
pubmed-meshheading:7962202-Mice,
pubmed-meshheading:7962202-Microfilament Proteins,
pubmed-meshheading:7962202-Microinjections,
pubmed-meshheading:7962202-Microvilli,
pubmed-meshheading:7962202-Myosins
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pubmed:year |
1994
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pubmed:articleTitle |
Brush border myosin-I microinjected into cultured cells is targeted to actin-containing surface structures.
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pubmed:affiliation |
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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