<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Dawoody Nejad, Ladan</dc:creator>
  <dc:creator>Stumpe, Michael</dc:creator>
  <dc:creator>Rauch, Monika</dc:creator>
  <dc:creator>Hemphill, Andrew</dc:creator>
  <dc:creator>Schneiter, Roger</dc:creator>
  <dc:creator>Bütikofer, Peter</dc:creator>
  <dc:creator>Serricchio, Mauro</dc:creator>
  <dc:date>2020-05-19</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Sphingosine-1-phosphate is a signaling molecule involved in the control of cell  migration, differentiation, survival and other physiological processes. This sphingolipid  metabolite can be degraded by the action of sphingosine-1-phosphate lyase (SPL) to  form hexadecenal and ethanolamine phosphate. The importance of SPL-mediated  ethanolamine phosphate formation has been characterized in only few cell types. We  show that in the protozoan parasite Trypanosoma brucei, expression of TbSpl is  essential for cell survival. Ablation of TbSpl expression increased sphingosine-1- phosphate levels and reduced de novo formation and steady-state levels of the  glycerophospholipid phosphatidylethanolamine (PE). Growth of TbSpl-depleted  parasites could be in part rescued by ethanolamine supplementation to the growth  medium, indicating that the main function of TbSpl is to provide ethanolamine  phosphate for PE synthesis. In contrast to most cell types analyzed, where SPL  localizes to the endoplasmic reticulum, we found by high-resolution microscopy that  TbSpl is a mitochondrial protein. In spite of its mitochondrial localization, TbSpl  depletion had no apparent effect on mitochondrial morphology but resulted in  aggregation of acidocalcisomes. Our results link mitochondria to sphingolipid  metabolism and suggest possible roles for PE in acidocalcisome function.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/308706</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/308706/files/sch_msp.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/308706/files/sch_msp_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-020-65248-x</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Scientific Reports. - 2020, vol. 10, no. 1, p. 8268</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">Mitochondrial sphingosine-1-phosphate lyase is essential for phosphatidylethanolamine synthesis and survival of Trypanosoma brucei</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
