Perreira, JillAker, AaronSavidis, GeorgeChin, Christopher R.McDougall, William M.Portmann, Jocelyn M.Meraner, PaulSmith, MilesRahman, MotiurBaker, Richard E.Gauthier, AnnickFranti, MichaelBrass, Abraham L.2022-08-232022-08-232015-08-042015-12-08Cell Rep. 2015 Aug 4;12(5):850-63. doi: 10.1016/j.celrep.2015.06.076. Epub 2015 Jul 23. <a href="http://dx.doi.org/10.1016/j.celrep.2015.06.076">Link to article on publisher's site</a>2211-1247 (Electronic)10.1016/j.celrep.2015.06.07626212330https://hdl.handle.net/20.500.14038/39828Human rhinovirus (HRV) causes upper respiratory infections and asthma exacerbations. We screened multiple orthologous RNAi reagents and identified host proteins that modulate HRV replication. Here, we show that RNASEK, a transmembrane protein, was needed for the replication of HRV, influenza A virus, and dengue virus. RNASEK localizes to the cell surface and endosomal pathway and closely associates with the vacuolar ATPase (V-ATPase) proton pump. RNASEK is required for endocytosis, and its depletion produces enlarged clathrin-coated pits (CCPs) at the cell surface. These enlarged CCPs contain endocytic cargo and are bound by the scissioning GTPase, DNM2. Loss of RNASEK alters the localization of multiple V-ATPase subunits and lowers the levels of the ATP6AP1 subunit. Together, our results show that RNASEK closely associates with the V-ATPase and is required for its function; its loss prevents the early events of endocytosis and the replication of multiple pathogenic viruses.en-US<p>Copyright © 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)</p>http://creativecommons.org/licenses/by-nc-nd/4.0/Cellular and Molecular PhysiologyMicrobial PhysiologyPathogenic MicrobiologyVirologyJournal Articlehttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3629&amp;context=oapubs&amp;unstamped=1https://escholarship.umassmed.edu/oapubs/26257920044oapubs/2625