Source:http://linkedlifedata.com/resource/pubmed/id/19403801
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2009-7-2
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| pubmed:abstractText |
Large conductance Ca(2+)-activated K(+) (BK(Ca)) channels encoded by the Slo1 gene (also known as KCNMA1) are physiologically important in a wide range of cell types and form complexes with a number of other proteins that affect their function. We performed a yeast two-hybrid screen to identify proteins that interact with BK(Ca) channels using a bait construct derived from domains in the extreme COOH-terminus of Slo1. A protein known as membrane-associated guanylate kinase with inverted orientation protein-1 (MAGI-1) was identified in this screen. MAGI-1 is a scaffolding protein that allows formation of complexes between certain transmembrane proteins, actin-binding proteins, and other regulatory proteins. MAGI-1 is expressed in a number of tissues, including podocytes and the brain. The interaction between MAGI-1 and BK(Ca) channels was confirmed by coimmunoprecipitation and glutathione S-transferase pull-down assays in differentiated cells of a podocyte cell line and in human embryonic kidneys (HEK)293T cells transiently coexpressing MAGI-1a and three different COOH-terminal Slo1 variants. Coexpression of MAGI-1 with Slo1 channels in HEK-293T cells results in a significant reduction in the surface expression of Slo1, as assessed by cell-surface biotinylation assays, confocal microscopy, and whole cell recordings. Partial knockdown of endogenous MAGI-1 expression by small interfering RNA (siRNA) in differentiated podocytes increased the surface expression of endogenous Slo1 as assessed by electrophysiology and cell-surface biotinylation assays, whereas overexpression of MAGI-1a reduced steady-state voltage-evoked outward current through podocyte BK(Ca) channels. These data suggest that MAGI-1 plays a role in regulation of surface expression of BK(Ca) channels in the kidney and possibly in other tissues.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
1522-1563
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
297
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
C55-65
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| pubmed:dateRevised |
2010-9-30
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| pubmed:meshHeading |
pubmed-meshheading:19403801-Animals,
pubmed-meshheading:19403801-Biotinylation,
pubmed-meshheading:19403801-Cell Line,
pubmed-meshheading:19403801-Cell Membrane,
pubmed-meshheading:19403801-Chick Embryo,
pubmed-meshheading:19403801-Down-Regulation,
pubmed-meshheading:19403801-Guanylate Kinase,
pubmed-meshheading:19403801-Humans,
pubmed-meshheading:19403801-Immunoprecipitation,
pubmed-meshheading:19403801-Large-Conductance Calcium-Activated Potassium Channel...,
pubmed-meshheading:19403801-Membrane Potentials,
pubmed-meshheading:19403801-Microscopy, Confocal,
pubmed-meshheading:19403801-Patch-Clamp Techniques,
pubmed-meshheading:19403801-Podocytes,
pubmed-meshheading:19403801-Protein Binding,
pubmed-meshheading:19403801-Protein Transport,
pubmed-meshheading:19403801-RNA Interference,
pubmed-meshheading:19403801-Recombinant Fusion Proteins,
pubmed-meshheading:19403801-Transfection,
pubmed-meshheading:19403801-Two-Hybrid System Techniques
|
| pubmed:year |
2009
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| pubmed:articleTitle |
MAGI-1 interacts with Slo1 channel proteins and suppresses Slo1 expression on the cell surface.
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| pubmed:affiliation |
Dept. of Biology and Biochemistry, Univ. of Houston, Houston, TX 77204-5001, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|