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UID:1142@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20221212T130000

DTEND;TZID=Asia/Jerusalem:20221212T140000

DTSTAMP:20221129T101143Z

URL:https://biology.technion.ac.il/en/seminars/dr-yoel-klug-sucking-up-the
 -fat-mechanism-of-lipid-droplet-formation/

SUMMARY:Dr. Yoel Klug-Sucking up the fat: mechanism of lipid droplet format
 ion [No Categories]
DESCRIPTION:Location: Faculty Of Biology Auditorium  Dr. Yoel Klug\n Affili
 ation: \n Host:Prof. Benjamin Podbilewicz  \n Abstract\n\nAll cells have e
 volved the means to store energy and thereby minimize the effects of fluct
 uations in nutrient availability. Cells store energy in the form of neutra
 l lipids\, such as triacylglycerol\, in specialized organelles called lipi
 d droplets (LDs). Besides storage of metabolic energy\, LDs play important
  roles in lipid and protein homeostasis and their deregulation is observed
  in a wide range of pathologies from obesity and atherosclerosis to diabet
 es. Despite their central roles in cellular metabolism\, the mechanisms of
  LD biogenesis remained largely unknown. LD biogenesis occurs at the endop
 lasmic reticulum and is coordinated by the evolutionary conserved membrane
  protein Seipin\, which is mutated in lipodystrophy. Despite the clear lin
 k between Seipin and LD formation\, how Seipin promoted and influenced LD 
 formation remained unclear.\n\nWe addressed this major open question in th
 e field. Using structural\, biochemical and molecular dynamics simulation 
 approaches we revealed the mechanism of LD formation by the yeast Seipin S
 ei1 and its membrane partner Ldb16. We showed that Sei1 luminal domain ass
 embles a homooligomeric ring\, which\, in contrast to other Seipins\, is u
 nable to concentrate triacylglycerol. Instead\, Sei1 positions Ldb16\, whi
 ch concentrates triacylglycerol within the Sei1 ring through critical hydr
 oxyl residues. Triacylglycerol recruitment to the complex is further promo
 ted by Sei1 transmembrane segments\, which also control Ldb16 stability. I
 n vivo studies using chimeras between yeast and human Seipin indicate that
  triacylglycerol-binding activity by Seipin is conserved across eukaryotes
 \, thus defining a unifying mechanism for Seipin mediated LD formation and
  lipid storage 
LOCATION:Faculty Of Biology Auditorium

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DTSTART:20221030T010000

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