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http://purl.uniprot.org/citations/15159385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15159385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15159385http://www.w3.org/2000/01/rdf-schema#comment"ATP-binding cassette (ABC)-type proteins are essential for bile formation in vertebrate liver. BSEP, MDR1, MDR2, and MRP2 ABC transporters are targeted to the apical (canalicular) membrane of hepatocytes where they execute ATP-dependent transport of bile acids, drugs, amphipathic cations, phospholipids, and conjugated organic anions, respectively. Changes in activity and abundance of transporters in the canalicular membrane regulate bile flow; however, little is known regarding cellular proteins that bind ABC transporters and regulate their trafficking. A yeast two-hybrid screen identified HAX-1 as a binding partner for BSEP, MDR1, and MDR2. The interactions were validated biochemically by glutathione S-transferase pull-down and co-immunoprecipitation assays. BSEP and HAX-1 were over-represented in rat liver subcellular fractions enriched for canalicular membrane vesicles, microsomes, and clathrin-coated vesicles. HAX-1 was bound to BSEP, MDR1, and MDR2 in canalicular membrane vesicles and co-localized with BSEP and MDR1 in the apical membrane of Madin-Darby canine kidney (MDCK) cells. RNA interference of HAX-1 increased BSEP levels in the apical membrane of MDCK cells by 71%. Pulse-chase studies indicated that HAX-1 depletion did not affect BSEP translation, post-translational modification, delivery to the plasma membrane, or half-life. HAX-1 depletion resulted in an increased peak of metabolically labeled apical membrane BSEP at 4 h and enhanced retention at 6 and 9 h. HAX-1 also interacts with cortactin. Expression of dominant negative cortactin increased steady state levels of BSEP 2-fold in the apical membrane of MDCK cells, as did expression of dominant negative EPS15. These findings suggest that HAX-1 and cortactin participate in BSEP internalization from the apical membrane."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m404337200"xsd:string
http://purl.uniprot.org/citations/15159385http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m404337200"xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Arias I.M."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Arias I.M."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Calderon G."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Calderon G."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Moseley J."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Moseley J."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Ortiz D.F."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Ortiz D.F."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Swift A.L."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/author"Swift A.L."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/pages"32761-32770"xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/pages"32761-32770"xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/title"Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells."xsd:string
http://purl.uniprot.org/citations/15159385http://purl.uniprot.org/core/title"Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells."xsd:string
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