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First published online May 15, 2009
Journal of Experimental Biology 212, 1630-1637 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.027375
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Tethering, recycling and activation of the epithelial sodium–proton exchanger, NHE3

R. Todd Alexander1 and Sergio Grinstein2,3,*

1 Department of Pediatrics, University of Alberta, Edmonton, Alberta, Canada, T6G 2R7
2 Program in Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada, M5G 1X8
3 Department of Biochemistry, University of Toronto, Ontario, Canada


Figure 1
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  		Fig. 1. The structure of NHE3 is divided into 12 transmembrane domains (residues 1–454) and a large cytosolic C-terminal domain (residues 455–831). The transmembrane domains implicated in ion transport are depicted in yellow and the domain responsible for inhibition by amiloride is depicted in pink (transmembrane domain IX). The diagram also indicates the putative binding sites for CHP (calcineurin homologous protein), ezrin and the NHERFs (sodium–hydrogen exchanger regulatory factor), the proton modifier sites (H+ sensor) and the sites that are phosphorylated by either protein kinase A (PKA) and serum and glucocorticoid kinase (SGK). DPP, dipeptidyl peptidase.

 

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  		Fig. 2. A model depicting the proposed subcellular distribution of NHE3 in epithelial cells. Note that NHE3 is located in two distinct locations on the apical membrane: most exchangers are tethered to the actin skeleton on microvilli whereas a smaller sub-population is found in the intramicrovillar space. The latter is more likely to internalize and exchange with endomembrane compartments. Endomembrane exchangers can recycle to the apical membrane but with complex kinetics that suggest the existence of fast- and slow-exchanging sub-compartments.

 

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