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

Détails

ID Serval
serval:BIB_27709
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells.
Périodique
American Journal of Physiology. Renal Physiology
Auteur(s)
Pribanic S., Gisler S.M., Bacic D., Madjdpour C., Hernando N., Sorribas V., Gantenbein A., Biber J., Murer H.
ISSN
0363-6127
Statut éditorial
Publié
Date de publication
2003
Volume
285
Numéro
4
Pages
784-791
Langue
anglais
Notes
Publication types: Journal Article
Résumé
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.
Mots-clé
Animals, Cell Line, Kidney Tubules, Proximal/cytology, Kidney Tubules, Proximal/metabolism, Male, Membrane Proteins/physiology, Mice, Mice, Inbred Strains, Neoplasm Proteins, Opossums, Sodium-Phosphate Cotransporter Proteins, Sodium-Phosphate Cotransporter Proteins, Type IIa, Symporters/physiology
Pubmed
Web of science
Création de la notice
19/11/2007 13:24
Dernière modification de la notice
20/08/2019 14:06
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