AKAP220 colocalizes with AQP2 in the inner medullary collecting ducts

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AKAP220 colocalizes with AQP2 in the inner medullary collecting ducts Rie Okutsu, Tatemitsu Rai, Akira Kikuchi, Mayuko Ohno, Keiko Uchida, Sei Sasaki, Shinichi Uchida Kidney International Volume 74, Issue 11, Pages 1429-1433 (December 2008) DOI: 10.1038/ki.2008.402 Copyright © 2008 International Society of Nephrology Terms and Conditions

Figure 1 AKAP220 is an AQP2-binding protein. (a) Whole AQP2 (1-271) binds to a partial AKAP220 (958-1306). A yeast colony expressing both AQP2 and AKAP220 could grow on the selection plate. (b) AQP2 without the C-terminal cytosolic region (1-224) could not bind to AKAP220. (c) Residues from 1098 to 1186 in AKAP220 are involved in the binding to AQP2. Kidney International 2008 74, 1429-1433DOI: (10.1038/ki.2008.402) Copyright © 2008 International Society of Nephrology Terms and Conditions

Figure 2 AKAP220 is present in the papillary collecting ducts of the kidney. (a) Total lysates from rat cortex (C), outer medulla (OM), and papilla (P) were separated by SDS–PAGE (27μg of protein per lane) and immunoblotted with anti-AKAP220 antibody and anti-actin antibody. AKAP220 was detected only in papilla. (b) Double immunofluorescence of AKAP220 and AQP2 in the rat kidney. AKAP220 was mainly present in the collecting ducts (upper panels) and colocalized with AQP2 in the subapical cytoplasmic region of the collecting ducts (indicated by arrows). (c) Double immunoelectron microscopy of AKAP220 and AQP2 in the rat kidney. Almost all large (20-nm) gold particles (AKAP220) were colocalized with small (10-nm) gold particles (AQP2; indicated by arrows). Original magnification (× 20,000). Kidney International 2008 74, 1429-1433DOI: (10.1038/ki.2008.402) Copyright © 2008 International Society of Nephrology Terms and Conditions

Figure 3 AKAP220 regulates the phosphorylation of AQP2 in COS cells. (a) Total cell lysates from COS cells transfected with either an empty vector or an HA-AKAP220 expression vector were immunoprecipitated with anti-HA antibody. The immunoprecipitates and total lysates were separated by SDS–PAGE and transferred to a nitrocellulose membrane that was then probed with antibodies to the catalytic and regulatory subunits of PKA. (b) Increased AQP2 phosphorylation by AKAP220. Demonstrable autoradiogram of phosphorylated AQP2 in COS cells with or without AKAP220 coexpression (upper panels). In the third lane from the left, AQP2 phosphorylation was not observed when serine 256 was mutated to alanine, indicating that Ser256 was the only phosphorylation site by PKA in this assay system. Full-length AKAP220 significantly increased AQP2 phosphorylation (second lane), whereas the mutant AKAP220 lacking the binding site to AQP2 did not increase AQP2 phosphorylation (fourth lane). Signal intensities of AQP2 phosphorylation measured by Image Gauge software (Fuji Film, Tokyo, Japan) were compared with the paired t-test (bar graph; P<0.01, n=4). Kidney International 2008 74, 1429-1433DOI: (10.1038/ki.2008.402) Copyright © 2008 International Society of Nephrology Terms and Conditions