Interaction of Integrin-linked Kinase with the Kidney Chloride/Bicarbonate Exchanger, kAE1

Kidney 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. Kidney 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. Anion exchanger 1 (AE1, 6The abbreviations used are: AE1, anion exchanger 1; kAE1, kidney AE1; eAE1, erythroid AE1; CH, calponin homology; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid; ILK, integrin-linked kinase; HA, hemagglutinin; BSA, bovine serum albumin; PBS, phosphate-buffered saline; MDCK, Madin-Darby canine kidney cells; dRTA, distal renal tubular acidosis; PH, pleckstrin homology. band 3, SLC4A1) is a bicarbonate transporter involved in maintaining acid-base homeostasis in the human body (1Godinich M.J. Jennings M.L. Curr. Opin Nephrol. Hypertens. 1995; 4: 398-401Crossref PubMed Scopus (14) Google Scholar). There are two human forms of AE1, erythroid (eAE1) and kidney (kAE1). eAE1 or band 3, is the major integral membrane glycoprotein of the erythrocyte, where it serves dual roles of Cl−/HCO3− exchange and cytoskeletal anchorage to red cell membranes (2Zhang D. Kiyatkin A. Bolin J.T. Low P.S. Blood. 2000; 96: 2925-2933Crossref PubMed Google Scholar). kAE1 is the basolateral Cl−/HCO3− exchanger of the acid-secreting α-intercalated cell of the kidney distal tubule (3Tanner M.J. Mol. Membr. Biol. 1997; 14: 155-165Crossref PubMed Scopus (187) Google Scholar). Transcription of eAE1 in erythroid precursors is under the control of an erythroid-specific promoter upstream of exon 1, whereas renal transcription arises from a distinct promoter within intron 3 of the AE1 gene (4Schofield A.E. Martin P.G. Spillett D. Tanner M.J. Blood. 1994; 84: 2000-2012Crossref PubMed Google Scholar). Thus, the resultant kidney transcript encodes the kAE1 polypeptide lacking 65 amino acids present at the N terminus of human eAE1 (5Brosius F.C. II I Alper S.L. Garcia A.M. Lodish H.F. J. Biol. Chem. 1989; 264: 7784-7787Abstract Full Text PDF PubMed Google Scholar). This structural alteration causes major functional between eAE1 and kAE1. The N terminus of eAE1 with and (3Tanner M.J. Mol. Membr. Biol. 1997; 14: 155-165Crossref PubMed Scopus (187) Google S.L. A. D. D. J. 1994; PubMed Scopus Google whereas the N terminus of kAE1 to these J. Biol. Chem. 1994; Full Text PDF PubMed Google Low P.S. J. Biol. Chem. 1995; Full Text Full Text PDF PubMed Scopus Google Scholar). The of the N-terminal domain of eAE1 revealed a of and as an N-terminal domain and a C-terminal domain (2Zhang D. Kiyatkin A. Bolin J.T. Low P.S. Blood. 2000; 96: 2925-2933Crossref PubMed Google is for kAE1. of eAE1 form the in the of a of in kAE1 may the of the cytosolic thereby protein the of in α-intercalated cells a protein anion exchanger was to with N-terminal kAE1 to eAE1 J. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). Human with human kAE1 and to the Mol. Membr. Biol. PubMed Scopus (14) Google Scholar). This to the with the N-terminal domain of kAE1 in human kidney of the AE1 gene distal renal tubular the of in α-intercalated cells J. Nephrol. 2000; 14: PubMed Scopus Google S.L. Google Scholar). AE1 with are residues and and an at the terminus AE1 to are and by the of and to the cell surface of the or the to the membrane of the basolateral membrane of cells which results in bicarbonate the basolateral membrane J. Google Scholar). in the N-terminal domain of kAE1 to with of the N terminus of kAE1 and C-terminal in the of the in Madin-Darby canine kidney cells, I that a within the kAE1 N terminus with the terminus for kAE1 basolateral A.M. Tanner M.J. J. PubMed Scopus Google Scholar). kidney a basolateral in the N-terminal F.C. J. PubMed Scopus Google Scholar). the that of kAE1 in to the basolateral membrane, the by which kAE1 is to the basolateral membrane of distal renal tubule cells and is kAE1 and it to that with kAE1. used two-hybrid screening of a human kidney to that with the domain of kAE1. that integrin-linked kinase (ILK), a serine/threonine kinase and actin-binding with the N-terminal domain of kAE1. 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PubMed Scopus Google Scholar). kAE1 with the terminus of ILK, kAE1 a of the N terminus of kAE1 and calponin and which the amino are and PubMed Scopus Google Full Text Full Text PDF PubMed Scopus Google it is that the of the N-terminal of kAE1 with the homology is at the The of the domain from was with the for amino acids of kAE1. The kAE1 domain is from the for the eAE1 domain (2Zhang D. Kiyatkin A. Bolin J.T. Low P.S. Blood. 2000; 96: 2925-2933Crossref PubMed Google Scholar). The domain in the N-terminal domain of kAE1 is to the domain in at the N terminus of the domain to of binding PubMed Scopus Google 1994; PubMed Scopus Google A. J. 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J. Full Text Full Text PDF PubMed Scopus Google Mol. Biol. PubMed Scopus Google and in human kidney cells with the of kAE1 in α-intercalated cells of the (3Tanner M.J. Mol. Membr. Biol. 1997; 14: 155-165Crossref PubMed Scopus (187) Google Scholar). confirmed these and of ILK and kAE1 at the basolateral surface of human α-intercalated shown is in these that an protein the of the that amino acids of human kAE1 to ILK to an amino with to of calponin and The to a calponin homology a protein previously shown to with identified the C-terminal kinase domain of ILK as kAE1 ILK, which amino acids into structural was as a protein J. PubMed Scopus Google Scholar). The N terminus of ILK by a pleckstrin and a C-terminal kinase catalytic domain J. PubMed Scopus Google Scholar). The at the N terminus of ILK with the Mol. Biol. PubMed Scopus Google whereas the C-terminal of ILK with and J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google J. PubMed Scopus Google J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). ILK catalytic activity is for with kinase J. A. PubMed Scopus Google J.T. D. J. J. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google and J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google ILK kinase activity was essential for with kAE1, with kAE1. that and with the terminus of ILK J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). ILK with as the in the C-terminal of ILK and ILK are likely distinct residues of the ILK terminus are for binding J. Biol. PubMed Scopus Google whereas binds to the domain ILK binds as as ILK, and the between an of the actin cytoskeleton J. Biol. 2000; PubMed Scopus Google Scholar). kAE1 may with ILK at a from and identified the in kAE1 that mediates ILK of the N terminus of kAE1 and the domain that amino residues of the kAE1 N terminus with The domain is a protein of amino identified at the N terminus of an actin-binding protein of PubMed Scopus Google J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The is between of from to Full Text Full Text PDF PubMed Scopus Google Scholar). the kAE1 domain is as it and with and calponin the identified as the structural between the N terminus of kAE1 and the domain from human Biol. 1997; 4: PubMed Scopus Google by The of the domain is of of a and of to present in the between the J. D. Full Text Full Text PDF PubMed Scopus Google Scholar). The for human eAE1 domain that the to residues of kAE1 to the of the domain 3, and are and are by of the to a surface two of the is to that the for the N terminus of kAE1 was by the eAE1 N terminus from the eAE1 (2Zhang D. Kiyatkin A. Bolin J.T. Low P.S. Blood. 2000; 96: 2925-2933Crossref PubMed Google Scholar). the eAE1 N terminus forms the of the domain shown in the of the of kAE1 the it is likely that the to the by of the eAE1 N that the of the kAE1 N-terminal the domain of Taken that the catalytic domain of ILK with the kAE1 domain in the N-terminal of kAE1. of ILK increased the Cl−/HCO3− exchange of This in transport activity with the of kAE1 cell surface that ILK associates with kAE1 early in biosynthesis, likely in the endoplasmic that the of kAE1 to the membrane may by with that actin may involved in cell surface of kAE1. that the association between ILK, and the to the actin cytoskeleton the domain J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). ILK may kAE1 to the actin cytoskeleton the results that the and from HEK 293 cells that the of the kAE1 to the actin cytoskeleton. 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Biol. 2000; PubMed Scopus Google the domain of with kAE1 for with ILK and to with actin The association of kAE1 with the actin cytoskeleton a and of kAE1 to the basolateral membrane of α-intercalated cells in the it to kAE1 or to the basolateral membrane, it is that are to the of kAE1 within the cell and control to the membrane. kAE1 two basolateral in the N terminus and in the at the N or terminus in of the that the of is essential for basolateral of kAE1 A.M. Tanner M.J. J. PubMed Scopus Google Scholar). The of the N-terminal basolateral of human kAE1 to The of kAE1 cell surface by ILK is to is to the cell surface and a of transport This to that may present in cells where is from HEK 293 cells J. J. PubMed Google Scholar). ILK may a for as as for kAE1. the of ILK in is The of ILK in with the of a band of human with together suggest that ILK is present in human in the the of ILK in ILK is as or A. J. Biol. PubMed Scopus Google J. 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