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dc.contributor.authorThitima Keskanokwongen_US
dc.contributor.authorHaley J. Shandroen_US
dc.contributor.authorDanielle E. Johnsonen_US
dc.contributor.authorSaranya Kittanakomen_US
dc.contributor.authorGonzalo L. Vilasen_US
dc.contributor.authorPaul Thorneren_US
dc.contributor.authorReinhart A F Reithmeieren_US
dc.contributor.authorVaraporn Akkarapatumwongen_US
dc.contributor.authorPa Thai Yenchitsomanusen_US
dc.contributor.authorJoseph R. Caseyen_US
dc.contributor.otherUniversity of Albertaen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherUniversity of Torontoen_US
dc.contributor.otherHospital for Sick Children University of Torontoen_US
dc.date.accessioned2018-08-24T01:40:46Z-
dc.date.available2018-08-24T01:40:46Z-
dc.date.issued2007-08-10en_US
dc.identifier.citationJournal of Biological Chemistry. Vol.282, No.32 (2007), 23205-23218en_US
dc.identifier.issn1083351Xen_US
dc.identifier.issn00219258en_US
dc.identifier.other2-s2.0-34548159996en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34548159996&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/24141-
dc.description.abstractKidney anion exchanger 1 (kAE1) mediates chloride/bicarbonate exchange at the basolateral membrane of kidney α-intercalated cells, thereby facilitating bicarbonate reabsorption into the blood. Human kAE1 lacks the N-terminal 65 residues of the erythroid form (AE1, band 3), which are essential for binding of cytoskeletal and cytosolic proteins. Yeast two-hybrid screening identified integrin-linked kinase (ILK), a serine/threonine kinase, and an actin-binding protein as an interacting partner with the N-terminal domain of kAE1. Interaction between kAE1 and ILK was confirmed in co-expression experiments in HEK 293 cells and is mediated by a previously unidentified calponin homology domain in the kAE1 N-terminal region. The calponin homology domain of kAE1 binds the C-terminal catalytic domain of ILK to enhance association of kAE1 with the actin cytoskeleton. Overexpression of ILK increased kAE1 levels at the cell surface as shown by flow cytometry, cell surface biotinylation, and anion transport activity assays. Pulse-chase experiments revealed that ILK associates with kAE1 early in biosynthesis, likely in the endoplasmic reticulum. ILK co-localized with kAE1 at the basolateral membrane of polarized Madin-Darby canine kidney cells and in α-intercalated cells of human kidneys. Taken together these results suggest that ILK and kAE1 traffic together from the endoplasmic reticulum to the basolateral membrane. ILK may provide a linkage between kAE1 and the underlying actin cytoskeleton to stabilize kAE1 at the basolateral membrane, resulting in higher levels of cell surface expression. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34548159996&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleInteraction of integrin-linked kinase with the kidney chloride/bicarbonate exchanger, kAE1en_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1074/jbc.M702139200en_US
Appears in Collections:Scopus 2006-2010

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