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2020-06-06Zeitschriftenartikel DOI: 10.3390/biom10060871
Yeast Sphingolipid-Enriched Domains and Membrane Compartments in the Absence of Mannosyldiinositolphosphorylceramide
dc.contributor.authorOliveira, Andreia
dc.contributor.authorSantos, Filipa
dc.contributor.authorTrigo Marquês, Joaquim
dc.contributor.authorPaulo, Pedro
dc.contributor.authorKorte, Thomas
dc.contributor.authorHerrmann, Andreas
dc.contributor.authorMarinho, H. Susana
dc.contributor.authorde Almeida, Rodrigo
dc.date.accessioned2022-05-19T08:03:17Z
dc.date.available2022-05-19T08:03:17Z
dc.date.issued2020-06-06none
dc.date.updated2020-07-11T01:42:48Z
dc.identifier.urihttp://edoc.hu-berlin.de/18452/25344
dc.description.abstractThe relevance of mannosyldiinositolphosphorylceramide [M(IP)2C] synthesis, the terminal complex sphingolipid class in the yeast Saccharomyces cerevisiae, for the lateral organization of the plasma membrane, and in particular for sphingolipid-enriched gel domains, was investigated by fluorescence spectroscopy and microscopy. We also addressed how changing the complex sphingolipid profile in the plasma membrane could influence the membrane compartments (MC) containing either the arginine/ H+ symporter Can1p (MCC) or the proton ATPase Pma1p (MCP). To achieve these goals, wild-type (wt) and ipt1Δ cells, which are unable to synthesize M(IP)2C accumulating mannosylinositolphosphorylceramide (MIPC), were compared. Living cells, isolated plasma membrane and giant unilamellar vesicles reconstituted from plasma membrane lipids were labelled with various fluorescent membrane probes that report the presence and organization of distinct lipid domains, global order, and dielectric properties. Can1p and Pma1p were tagged with GFP and mRFP, respectively, in both yeast strains, to evaluate their lateral organization using confocal fluorescence intensity and fluorescence lifetime imaging. The results show that IPT1 deletion strongly affects the rigidity of gel domains but not their relative abundance, whereas no significant alterations could be perceived in ergosterol-enriched domains. Moreover, in these cells lacking M(IP)2C, a clear alteration in Pma1p membrane distribution, but no significant changes in Can1p distribution, were observed. Thus, this work reinforces the notion that sphingolipid-enriched domains distinct from ergosterol-enriched regions are present in the S. cerevisiae plasma membrane and suggests that M(IP)2C is important for a proper hydrophobic chain packing of sphingolipids in the gel domains of wt cells. Furthermore, our results strongly support the involvement of sphingolipid domains in the formation and stability of the MCP, possibly being enriched in this compartment.eng
dc.language.isoengnone
dc.publisherHumboldt-Universität zu Berlin
dc.rights(CC BY 4.0) Attribution 4.0 Internationalger
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject<i>Saccharomyces cerevisiae</i>eng
dc.subjectmembrane compartmentseng
dc.subjectsphingolipidseng
dc.subjectPma1peng
dc.subjectCan1peng
dc.subjectfluorescence lifetime imaging microscopy (FLIM)eng
dc.subjectfungal plasma membraneeng
dc.subjectinositolphosphorylceramideseng
dc.subjectfluorescence spectroscopyeng
dc.subjectgiant unilamellar vesicles (GUVs)eng
dc.subject.ddc570 Biologienone
dc.titleYeast Sphingolipid-Enriched Domains and Membrane Compartments in the Absence of Mannosyldiinositolphosphorylceramidenone
dc.typearticle
dc.identifier.urnurn:nbn:de:kobv:11-110-18452/25344-1
dc.identifier.doi10.3390/biom10060871none
dc.identifier.doihttp://dx.doi.org/10.18452/24677
dc.type.versionpublishedVersionnone
local.edoc.container-titleBiomoleculesnone
local.edoc.pages24none
local.edoc.type-nameZeitschriftenartikel
local.edoc.institutionLebenswissenschaftliche Fakultätnone
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-publisher-nameMDPInone
local.edoc.container-publisher-placeBaselnone
local.edoc.container-volume10none
local.edoc.container-issue6none
dc.description.versionPeer Reviewednone
local.edoc.container-articlenumber871none
dc.identifier.eissn2218-273X

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