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http://purl.uniprot.org/citations/23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23255603http://www.w3.org/2000/01/rdf-schema#comment"The large conductance voltage- and Ca(2+)-activated K(+) channel (MaxiK, BK(Ca), BK) is composed of four pore-forming α-subunits and can be associated with regulatory β-subunits. One of the functional roles of MaxiK is to regulate vascular tone. We recently found that the MaxiK channel from coronary smooth muscle is trans-inhibited by activation of the vasoconstricting thromboxane A(2) prostanoid receptor (TP), a mechanism supported by MaxiK α-subunit (MaxiKα)-TP physical interaction. Here, we examined the role of the MaxiK β1-subunit in TP-MaxiK association. We found that the β1-subunit can by itself interact with TP and that this association can occur independently of MaxiKα. Subcellular localization analysis revealed that β1 and TP are closely associated at the cell periphery. The molecular mechanism of β1-TP interaction involves predominantly the β1 extracellular loop. As reported previously, TP activation by the thromboxane A(2) analog U46619 caused inhibition of MaxiKα macroscopic conductance or fractional open probability (FP(o)) as a function of voltage. However, the positive shift of the FP(o) versus voltage curve by U46619 relative to the control was less prominent when β1 was coexpressed with TP and MaxiKα proteins (20 ± 6 mV, n = 7) than in cells expressing TP and MaxiKα alone (51 ± 7 mV, n = 7). Finally, β1 gene ablation reduced the EC(50) of the U46619 agonist in mediating aortic contraction from 18 ± 1 nm (n = 12) to 9 ± 1 nm (n = 12). The results indicate that the β1-subunit can form a tripartite complex with TP and MaxiKα, has the ability to associate with each protein independently, and diminishes U46619-induced MaxiK channel trans-inhibition as well as vasoconstriction."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.426585"xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Lu R."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Koh H."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Jiang Z."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Alioua A."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Stefani E."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Garcia-Valdes J."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/author"Toro L."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/pages"3668-3677"xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/title"The beta1-subunit of the MaxiK channel associates with the thromboxane A2 receptor and reduces thromboxane A2 functional effects."xsd:string
http://purl.uniprot.org/citations/23255603http://purl.uniprot.org/core/volume"288"xsd:string
http://purl.uniprot.org/citations/23255603http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23255603
http://purl.uniprot.org/citations/23255603http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23255603
http://purl.uniprot.org/uniprot/#_P21731-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603
http://purl.uniprot.org/uniprot/#_Q05C92-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603
http://purl.uniprot.org/uniprot/#_Q16558-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603
http://purl.uniprot.org/uniprot/#_Q0VAA9-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603
http://purl.uniprot.org/uniprot/#_Q0VAB0-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603
http://purl.uniprot.org/uniprot/#_P30987-mappedCitation-23255603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23255603