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The Sodium/Proton Exchanger NHE8 Regulates Late Endosomal Morphology and Function
<span title="2010-10-15">2010</span>
<i title="American Society for Cell Biology (ASCB)">
<a target="_blank" rel="noopener" href="https://fatcat.wiki/container/btmjitlxs5by3dntmzk67gakxi" style="color: black;">Molecular Biology of the Cell</a>
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The pH and lumenal environment of intracellular organelles is considered essential for protein sorting and trafficking through the cell. We provide the first evidence that a mammalian NHE sodium (potassium)/proton exchanger, NHE8, plays a key role in the control of protein trafficking and endosome morphology. At steady state, the majority of epitope-tagged NHE8 was found in the trans-Golgi network of HeLa M-cells, but a proportion was also localized to multivesicular bodies (MVBs). Depletion of
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<a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1091/mbc.e09-12-1053">doi:10.1091/mbc.e09-12-1053</a>
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... NHE8 in HeLa M-cells with siRNA resulted in the perturbation of MVB protein sorting, as shown by an increase in epidermal growth factor degradation. Additionally, NHE8-depleted cells displayed striking perinuclear clustering of endosomes and lysosomes, and there was a ninefold increase in the cellular volume taken up by LAMP1/ LBPA-positive, dense MVBs. Our data points to a role for the ion exchange activity of NHE8 being required to maintain endosome morphology, as overexpression of a nonfunctional point mutant protein (NHE8 E225Q) resulted in phenotypes similar to those seen after siRNA depletion of endogenous NHE8. Interestingly, we found that depletion of NHE8, despite its function as a sodium (potassium)/proton antiporter, did not affect the overall pH inside dense MVBs.
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