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Phospholipids containing ether-bound hydrocarbon-chains are essential for efficient phagocytosis and neutral lipids of the ester-type perturb development in Dictyostelium

dc.date.accessioned2020-08-28T08:11:52Z
dc.date.available2020-08-28T08:11:52Z
dc.date.issued2020-07-16
dc.identifierdoi:10.17170/kobra-202008271662
dc.identifier.urihttp://hdl.handle.net/123456789/11741
dc.description.sponsorshipGefördert durch den Publikationsfonds der Universität Kasselger
dc.language.isoengeng
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectendoplasmic reticulumeng
dc.subjectperoxisomeseng
dc.subjectlipid dropletseng
dc.subjectGPATeng
dc.subjectDHAPATeng
dc.subjectmacropinocytosiseng
dc.subject.ddc570
dc.titlePhospholipids containing ether-bound hydrocarbon-chains are essential for efficient phagocytosis and neutral lipids of the ester-type perturb development in Dictyosteliumeng
dc.typeAufsatz
dcterms.abstractLipids are the building blocks for cellular membranes; they provide signalling molecules for membrane dynamics and serve as energy stores. One path of their synthesis is initiated by glycerol-3-phosphate acyltransferase (GPAT), which in Dictyostelium resides on the endoplasmic reticulum. When an excess of fatty acids is present, it redistributes to storage organelles, the lipid droplets. Mutants, where the GPAT was eliminated by homologous recombination, produce fewer lipid droplets and are almost devoid of triacylglycerols (TAG), rendering them more resistant to cell death and cell loss in the developmental stages preceding fruiting body formation. The enzyme most closely related to GPAT is called FARAT, because it combines a fatty acyl-reductase (FAR) and an acyltransferase (AT) domain in its sequence. The protein is confined to the lumen of the peroxisome, where it transfers a fatty acid to dihydroxyacetone-phosphate initiating the synthesis of ether lipids, later completed at the endoplasmic reticulum. A mutant lacking FARAT produces lipid droplets that are devoid of the storage lipid monoalkyl-diacyl-glycerol (MDG), but the efficiency of spore formation in the developmental cycle is largely unaltered. Instead, these mutants are strongly impaired in phagocytosis of yeast particles, which is attributed to reduced synthesis of membrane phospholipids containing ether-linked chains.eng
dcterms.accessRightsopen access
dcterms.creatorKappelt, Frederik
dcterms.creatorDu Ma, Xiaoli
dcterms.creatorHasna, Bassam Abou
dcterms.creatorKornke, Jessica Maria
dcterms.creatorManiak, Markus
dc.relation.doidoi:10.1242/bio.052126
dc.subject.swdPhospholipideger
dc.subject.swdEndoplasmatisches Retikulumger
dc.subject.swdPeroxisomger
dc.subject.swdAcyltransferasenger
dc.subject.swdPinocytoseger
dc.type.versionpublishedVersion
dcterms.source.identifierEISSN 2046-6390
dcterms.source.issueIssue 7
dcterms.source.journalBiology openeng
dcterms.source.pageinfobio052126
dcterms.source.volumeVolume 9
kup.iskupfalse


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