Source:http://linkedlifedata.com/resource/pubmed/id/12923176
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
43
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| pubmed:dateCreated |
2003-10-20
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| pubmed:abstractText |
The role of filamins in actin cross-linking and membrane stabilization is well established, but recently their ability to interact with a variety of transmembrane receptors and signaling proteins has led to speculation of additional roles in scaffolding and signal transduction. Here we report a direct interaction between filamin-A and Kir2.1, an isoform of inwardly rectifying potassium channel expressed in vascular smooth muscle and an important regulator of vascular tone. Yeast two-hybrid screening of a porcine coronary artery cDNA library using the carboxyl terminus of Kir2.1 as bait yielded cDNA encoding a fragment of filamin-A (residues 2481-2647). Interaction between filamin-A and Kir2.1 was confirmed by in vitro overlay assay of membrane-bound Kir2.1 with glutathione S-transferase fusion protein of the isolated filamin clone. Additionally, antibodies directed against Kir2.1 coimmunoprecipitated filamin-A from arterial smooth muscle cell lysates, and immunocytochemical analysis of individual arterial smooth muscle cells showed that Kir2.1 and filamin co-localize in "hotspots" at the cell membrane. Interaction with filamin-A was found to have no effect on Kir2.1 channel behavior but, rather, increased the number of functional channels resident within the membrane. We conclude that filamin-A is potentially an important regulator of Kir2.1 surface expression and location within vascular smooth muscle.
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| 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/Contractile Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/filamins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
24
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| pubmed:volume |
278
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
41988-97
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12923176-Actins,
pubmed-meshheading:12923176-Amino Acid Sequence,
pubmed-meshheading:12923176-Animals,
pubmed-meshheading:12923176-Cell Line, Tumor,
pubmed-meshheading:12923176-Contractile Proteins,
pubmed-meshheading:12923176-Coronary Vessels,
pubmed-meshheading:12923176-DNA, Complementary,
pubmed-meshheading:12923176-Electrophysiology,
pubmed-meshheading:12923176-Humans,
pubmed-meshheading:12923176-Immunohistochemistry,
pubmed-meshheading:12923176-Microfilament Proteins,
pubmed-meshheading:12923176-Muscle, Smooth, Vascular,
pubmed-meshheading:12923176-Mutation,
pubmed-meshheading:12923176-Myocytes, Smooth Muscle,
pubmed-meshheading:12923176-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:12923176-Precipitin Tests,
pubmed-meshheading:12923176-Protein Binding,
pubmed-meshheading:12923176-Swine,
pubmed-meshheading:12923176-Two-Hybrid System Techniques
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| pubmed:year |
2003
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| pubmed:articleTitle |
Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1.
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| pubmed:affiliation |
Department of Cell Physiology and Pharmacology, University of Leicester, P. O. Box 138, Leicester LE1 9HN, United Kingdom. ljs17@le.ac.uk
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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