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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1995-3-9
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pubmed:abstractText |
Potassium-depleted fibroblasts are unable to develop polarized morphology and lack coated pits. Experiments were carried out to measure internalization of fibronectin receptors (FNR) in potassium-depleted cells and possible association of FNR with AP-2 complexes after adding potassium back to the cells, which restores cell polarization. AP-2 complexes are the cell surface component of coated pits that contain both clathrin and membrane receptor binding domains. Potassium-depleted fibroblasts endocytosed antibody-tagged FNR and also internalized fluorescent fibronectin that previously had been adsorbed to the substratum. During cell polarization, antibody-tagged FNR reorganized into fibrillar structures along stress fibers beginning from nucleation sites at cell margins. Plasma membrane AP-2 complexes, which were undetectable in potassium-depleted cells, reappeared at the cell surface above the nucleus and then spread toward the cell margins. The results show that endocytosis of FNR can occur at least partially by a coated pit-independent mechanism.
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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/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
216
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
299-309
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7843274-Actins,
pubmed-meshheading:7843274-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:7843274-Cell Polarity,
pubmed-meshheading:7843274-Cells, Cultured,
pubmed-meshheading:7843274-Endocytosis,
pubmed-meshheading:7843274-Fibroblasts,
pubmed-meshheading:7843274-Fibronectins,
pubmed-meshheading:7843274-Humans,
pubmed-meshheading:7843274-Nerve Tissue Proteins,
pubmed-meshheading:7843274-Phosphoproteins,
pubmed-meshheading:7843274-Potassium,
pubmed-meshheading:7843274-Receptors, Fibronectin,
pubmed-meshheading:7843274-Skin
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pubmed:year |
1995
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pubmed:articleTitle |
Fibronectin receptor internalization and AP-2 complex reorganization in potassium-depleted fibroblasts.
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pubmed:affiliation |
Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas 75235.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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