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VERSION:2.0
CALSCALE:GREGORIAN
PRODID:UW-Madison-Physics-Events
BEGIN:VEVENT
SEQUENCE:0
UID:UW-Physics-Event-2741
DTSTART:20120918T170500Z
DURATION:PT1H0M0S
DTSTAMP:20260418T052800Z
LAST-MODIFIED:20120829T195256Z
LOCATION:4274 Chamberlin (refreshments will be served)
SUMMARY:The discovery of the ER-based acetylation machinery: from agin
 g to Alzheimer's disease ... cancer too?\, Chaos & Complex Systems Sem
 inar\, Luigi Puglielli\, UW Department of Medicine
DESCRIPTION:Our group recently reported that mammalian cells are able 
 to acetylate the Ne-lysine residue of nascent membrane proteins in the
  lumen of the endoplasmic reticulum (ER). This event was initially dis
 covered while studying the mechanisms that regulate the levels of b-si
 te APP cleaving enzyme 1 (BACE1)\, a type I membrane protein that is i
 nvolved in the pathogenesis of AlzheimeraEuroTMs disease. However\, it
  is now clear that this process is not limited to BACE1. In fact\, oth
 er membrane and secreted proteins as well as ER-resident proteins that
  are involved with synthesis and folding of nascent proteins in the ER
  lumen are also acetylated. Here\, I will describe the biochemical pro
 perties of the individual components of the ER-based acetylation machi
 nery and their impact on different neurodegenerative diseases\, includ
 ing AlzheimeraEuroTMs disease and spastic paraplegias. I will also dis
 cuss the initial characterization of a newly-generated animal model sh
 owing a possible impact of the ER-based acetylation machinery on the b
 iology of the immune system as well as the risk for cancer.
URL:https://www.physics.wisc.edu/events/?id=2741
END:VEVENT
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