ID 106038
Author
Yamada, Fumiyo Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
Horie, Daisuke Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
Nakamura, Asako Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
Tanimura, Ayako Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School KAKEN Search Researchers
Yamamoto, Hironori Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School KAKEN Search Researchers
Segawa, Hiroko Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Ito, Mikiko University of Hyogo School of Human Science and Environment
Miyamoto, Ken-ichi Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Taketani, Yutaka Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Takeda, Eiji Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
ERM family
ezrin, parathyroid hormone
phosphate homeostasis
sodium-dependent phosphate transporter
sodium-proton exchanger related factors
Content Type
Journal Article
Description
Type IIa sodium-dependent phosphate transporter (NaPi-IIa) is responsible for renal phosphate reabsorption and maintenance of systemic phosphate homeostasis in mammals. Macromolecular complex formation of NaPi-IIa with sodium-proton exchanger related factor-1 (NHERF-1) and ezrin is important for apical membrane localization in the proximal tubular cells. Here, we investigated the interactions of the ezrin phosphomimetic mutation of serine to aspartic acid at 249 with NHERF-1 and the inhibition of apical membrane localization of NaPi-IIa. In vitro phosphorylation analysis revealed that serine 249 of human ezrin serves as a phosphorylation site for protein kinase A. The Nterminal half of ezrin had a dominant negative effect on the phosphate transport activity and inhibited the apical localization of NaPi-IIa in renal proximal tubular cells. We found that the phosphomimetic S249D mutant interfered with the inhibitory effects of the dominant negative mutant on the transport and localization of NaPi-IIa. The S249D mutant also inhibited the interaction with NHERF-1. Therefore, serine 249 of ezrin can play important roles in the regulation of the complex formation and membrane localization of NaPi-IIa.
Journal Title
The journal of medical investigation : JMI
ISSN
13431420
NCID
AA11166929
Volume
60
Issue
1-2
Start Page
27
End Page
34
Sort Key
27
Published Date
2013-02
EDB ID
FullText File
language
eng
TextVersion
Publisher
departments
Oral Sciences
Medical Sciences