Browse by author
Lookup NU author(s): Dr Francesca Di Sole
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The Na+/H+-exchanger 3 (NHE3) is essential for regulation of Na+ transport in the renal and intestinal epithelium. Although changes in cell surface abundance control NHE3 function, the molecular signals that regulate NHE3 surface expression are not well defined. We found that overexpression of the calcineurin homologous protein-1 (CHP1) in opossum kidney cells increased NHE3 transport activity, surface protein abundance, and ezrin phosphorylation. CHP1 knockdown by small interfering RNA had the opposite effects. Overexpression of wild-type ezrin increased both NHE3 transport activity and surface protein abundance, confirming that NHE3 is downstream of ezrin. Expression of a pseudophosphorylated ezrin enhanced these effects, whereas expression of an ezrin variant that could not be phosphorylated prevented the downstream effects on NHE3. Furthermore, CHP1 knockdown reversed the activation of NHE3 by wild-type ezrin but not by the pseudophosphorylated ezrin. Taken together, these results demonstrate that CHP1 increases NHE3 abundance and constitutive function in a manner dependent on ezrin phosphorylation.
Author(s): Di Sole F, Babich V, Moe OW
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: Journal of the American Society of Nephrology: Experimental Biology 2008 Annual Meeting
Year of Conference: 2009
Pages: 1776-1786
ISSN: 1555-9041
Publisher: American Society of Nephrology
URL: http://dx.doi.org/10.1681/ASN.2008121255
DOI: 10.1681/ASN.2008121255
Library holdings: Search Newcastle University Library for this item
ISBN: 1555905X
