ID 106038
著者
ヤマダ, フミヨ Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
ホリエ, ダイスケ Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
ナカムラ, アサコ Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
谷村, 綾子 Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School KAKEN研究者をさがす
山本, 浩範 Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School KAKEN研究者をさがす
瀬川, 博子 Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School 徳島大学 教育研究者総覧 KAKEN研究者をさがす
イトウ, ミキコ University of Hyogo School of Human Science and Environment
宮本, 賢一 Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School 徳島大学 教育研究者総覧 KAKEN研究者をさがす
竹谷, 豊 Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School 徳島大学 教育研究者総覧 KAKEN研究者をさがす
武田, 英二 Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School 徳島大学 教育研究者総覧 KAKEN研究者をさがす
キーワード
ERM family
ezrin, parathyroid hormone
phosphate homeostasis
sodium-dependent phosphate transporter
sodium-proton exchanger related factors
資料タイプ
学術雑誌論文
抄録
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.
掲載誌名
The journal of medical investigation : JMI
ISSN
13431420
cat書誌ID
AA11166929
60
1-2
開始ページ
27
終了ページ
34
並び順
27
発行日
2013-02
EDB ID
フルテキストファイル
言語
eng
著者版フラグ
出版社版
部局
歯学系
医学系