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Am J Physiol Cell Physiol 287: C844-C850, 2004; doi:10.1152/ajpcell.00094.2004
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INVITED REVIEW

Na+/H+ exchanger NHE1 as plasma membrane scaffold in the assembly of signaling complexes

Martin Baumgartner, Hitesh Patel, and Diane L. Barber

Department of Stomatology, University of California, San Francisco, California 94143

The plasma membrane Na+/H+ exchanger NHE1 has an established function in intracellular pH and cell volume homeostasis by catalyzing electroneutral influx of extracellular Na+ and efflux of intracellular H+. A second function of NHE1 as a structural anchor for actin filaments through its direct binding of the ezrin, radixin, and moesin (ERM) family of actin-binding proteins was recently identified. ERM protein binding and actin anchoring by NHE1 are necessary to retain the localization of NHE1 in specialized plasma membrane domains and to promote cytoskeleton-dependent processes, including actin filament bundling and cell-substrate adhesions. This review explores a third function of NHE1, as a plasma membrane scaffold in the assembly of signaling complexes. Through its coordinate functions in H+ efflux, actin anchoring, and scaffolding, we propose that NHE1 promotes protein interactions and activities, assembles signaling complexes in specialized plasma membrane domains, and coordinates divergent signaling pathways.

hydrogen ion efflux; intracellular pH; molecular scaffold


Address for reprint requests and other correspondence: D. L. Barber, Box 0512, Univ. of California, San Francisco, 513 Parnassus Ave., San Francisco, CA 94143 (E-mail: barber{at}itsa.ucsf.edu)




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