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Am J Physiol Renal Physiol (July 1, 2003). doi:10.1152/ajprenal.00109.2003
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Submitted on March 19, 2003
Accepted on June 26, 2003

Interactions of MAP17 with the NaPi-IIa / PDZK1 protein complex in renal proximal tubular cells

Sandra Pribanic1, Serge Mike Gisler1, Desa Bacic2, Caveh Madjdpour3, Nati Hernando1, Victor Sorribas4, Andrea Gantenbein2, Jurg Biber1*, and Heini Murer1

1 Institute of Physiology, University Zurich, Zurich, ZH, Switzerland
2 InstituteAnatomy, University Zurich, Zurich, ZH, Switzerland
3 Institute of Physiology, University Zurich, Zurich, ZH, Switzerland; InstituteAnatomy, University Zurich, Zurich, ZH, Switzerland
4 Department of Toxicology, University Zaragoza, Zaragoza, Spain

* To whom correspondence should be addressed. E-mail: JuergBiber{at}access.unizh.ch.

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 carboxy-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 amino-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 is also expressed in normal kidneys. Results obtained by various in-vitro analyses suggested that MAP17 interacts with the 4th 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 OK-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 i) interacts with PDZK1 only, ii) associates with the N-terminus of NaPi-IIa within the PDZK1/NaPi-IIa/MAP17 complex, and iii) acts as an apical anchoring site for PDZK1.




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