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Am J Physiol Renal Physiol 285: F784-F791, 2003. First published July 1, 2003; doi:10.1152/ajprenal.00109.2003
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Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells

Sandra Pribanic,1 Serge Mike Gisler,1 Desa Bacic,1,2 Caveh Madjdpour,1,2 Nati Hernando,1 Victor Sorribas,3 Andrea Gantenbein,2 Jürg Biber,1 and Heini Murer1

Institutes of 1Physiology and 2Anatomy, University of Zürich, 8057 Zürich, Switzerland; and 3Department of Toxicology, University of Zaragoza, E-50.013 Zaragoza, Spain

Submitted 19 March 2003 ; accepted in final form 26 June 2003

An essential role in phosphate homeostasis is played by Na/Pi cotransporter IIa that is localized in the brush borders of renal proximal tubular cells. Recent studies identified several PDZ proteins interacting with the COOH-terminal tail of NaPi-IIa, such as PDZK1 and NHERF-1. Here, by using yeast two-hybrid screen of mouse kidney cDNA library, we attempted to find proteins interacting with the NH2-terminal part of NaPi-IIa. We identified MAP17, a 17-kDa membrane protein that has been described to be associated with various human carcinomas, but it is also expressed in normal kidneys. Results obtained by various in vitro analyses suggested that MAP17 interacts with the fourth domain of PDZK1 but not with other PDZ proteins localized in proximal tubular brush borders. As revealed by immunofluorescence, MAP17 was abundant in S1 but almost absent in S3 segments. No alterations of the apical abundance of MAP17 were observed after maneuvers undertaken to change the content of NaPi-IIa (parathyroid hormone treatment, different phosphate diets). In agreement, no change in the amount of MAP17 mRNA was observed. Results obtained from transfection studies using opossum kidney cells indicated that the apical localization of MAP17 is independent of PDZK1 but that MAP17 is required for apical localization of PDZK1. In summary, we conclude that MAP17 1) interacts with PDZK1 only, 2) associates with the NH2 terminus of NaPi-IIa within the PDZK1/NaPi-IIa/MAP17 complex, and 3) acts as an apical anchoring site for PDZK1.

interacting proteins; Na/Pi cotransport; PDZ proteins; NHERF-1; opossum kidney cells


Address for reprint requests and other correspondence: J. Biber, Institute of Physiology, Univ. of Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland (E-mail: JuergBiber{at}access.unizh.ch).




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