| Автор | Putney, L. K. |
| Автор | Denker, S. P. |
| Автор | Barber, D. L. |
| Дата выпуска | 2002 |
| dc.description | ▪ Abstract The NHE family of ion exchangers includes six isoforms (NHE1–NHE6) that function in an electroneutral exchange of intracellular H<sup>+</sup> for extracellular Na<sup>+</sup>. This review focuses on the only ubiquitously expressed isoform, NHE1, which is localized at the plasma membrane where it plays a critical role in intracellular pH (pHi) and cell volume homeostasis. All NHE isoforms share a similar topology: an N-terminus of 12 transmembrane (TM) α-helices that collectively function in ion exchange, and a C-terminal cytoplasmic regulatory domain that modulates transport activity by the TM domain. Extracellular signals, mediated by diverse classes of cell-surface receptors, regulate NHE1 activity through distinct signaling networks that converge to directly modify the C-terminal regulatory domain. Modifications in the C-terminus, including phosphorylation and the binding of regulatory proteins, control transport activity by altering the affinity of the TM domain for intracellular H<sup>+</sup>. Recently, it was determined that NHE1 also functions as a membrane anchor for the actin-based cytoskeleton, independently of its role in ion translocation. Through its effects on pHi homeostasis, cell volume, and the actin cortical network, NHE1 regulates a number of cell behaviors, including adhesion, shape determination, migration, and proliferation. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | THE CHANGING FACE OF THE Na<sup>+</sup>/H<sup>+</sup> EXCHANGER, NHE1: Structure, Regulation, and Cellular Actions |
| DOI | 10.1146/annurev.pharmtox.42.092001.143801 |
| Print ISSN | 0362-1642 |
| Журнал | Annual Review of Pharmacology and Toxicology |
| Том | 42 |
| Первая страница | 527 |
| Последняя страница | 552 |
| Аффилиация | Putney, L. K.; Department of Stomatology, University of California, San Francisco, HSW 604, San Francisco, California 94143-0512; e-mail: barber@itsa.ucsf.edu lputney@itsa.ucsf.edu sdenker@itsa.ucsf.edu |
