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dc.contributor.authorGarten, Matthias
dc.contributor.authorNasamu, Armiyaw S.
dc.contributor.authorZimmerberg, Joshua
dc.contributor.authorGoldberg, Daniel E.
dc.contributor.authorBeck, Josh R.
dc.contributor.authorNiles, Jacquin
dc.date.accessioned2018-11-20T14:48:20Z
dc.date.available2018-11-20T14:48:20Z
dc.date.issued2018-08
dc.date.submitted2018-04
dc.identifier.issn2058-5276
dc.identifier.urihttp://hdl.handle.net/1721.1/119216
dc.description.abstractIntraerythrocytic malaria parasites reside within a parasitophorous vacuolar membrane (PVM) generated during host cell invasion. Erythrocyte remodelling and parasite metabolism require the export of effector proteins and transport of small molecules across this barrier between the parasite surface and host cell cytosol. Protein export across the PVM is accomplished by the Plasmodium translocon of exported proteins (PTEX) consisting of three core proteins, the AAA+ ATPase HSP101 and two additional proteins known as PTEX150 and EXP2. Inactivation of HSP101 and PTEX150 arrests protein export across the PVM, but the contribution of EXP2 to parasite biology is not well understood. A nutrient permeable channel in the PVM has also been characterized electrophysiologically, but its molecular identity is unknown. Here, using regulated gene expression, mutagenesis and cell-attached patch-clamp measurements, we show that EXP2, the putative membrane-spanning channel of PTEX, serves dual roles as a protein-conducting channel in the context of PTEX and as a channel able to facilitate nutrient passage across the PVM independent of HSP101. Our data suggest a dual functionality for a channel operating in its endogenous context.en_US
dc.language.isoen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofhttps://doi.org/10.1038/s41564-018-0222-7en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourceNiles, Jacquin Cen_US
dc.titleEXP2 is a nutrient-permeable channel in the vacuolar membrane of Plasmodium and is essential for protein export via PTEXen_US
dc.title.alternativeEXP2 is a nutrient-permeable channel in the vacuolar membrane of Plasmodium and is essential for protein export via PTEXen_US
dc.typeArticleen_US
dc.identifier.citationGarten, Matthias et al. “EXP2 Is a Nutrient-Permeable Channel in the Vacuolar Membrane of Plasmodium and Is Essential for Protein Export via PTEX.” Nature Microbiology 3, 10 (August 2018): 1090–1098 © 2018 Nature Publishing Groupen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.approverNiles, Jacquinen_US
dc.contributor.mitauthorNiles, Jacquin
dc.relation.journalNature Microbiologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsGarten, Matthias; Nasamu, Armiyaw S.; Niles, Jacquin C.; Zimmerberg, Joshua; Goldberg, Daniel E.; Beck, Josh R.en_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-6250-8796
mit.licenseOPEN_ACCESS_POLICYen_US


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