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VERSION:2.0
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PRODID:UW-Physics-TWaP
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SEQUENCE:0
UID:UW-Physics-Event-2741
DTSTART:20120918T120500
DURATION:PT1H0M0S
LOCATION:4274 Chamberlin (refreshments will be served)
SUMMARY:The discovery of the ER-based acetylation machinery: from aging to Alzheimer's disease ... cancer too?\, Chaos & Complex Systems Seminar\, 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 discovered while studying the mechanisms that regulate the levels of b-site APP cleaving enzyme 1 (BACE1)\, a type I membrane protein that is involved in the pathogenesis of AlzheimeraEuroTMs disease. However\, it is now clear that this process is not limited to BACE1. In fact\, other 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 properties of the individual components of the ER-based acetylation machinery and their impact on different neurodegenerative diseases\, including AlzheimeraEuroTMs disease and spastic paraplegias. I will also discuss the initial characterization of a newly-generated animal model showing a possible impact of the ER-based acetylation machinery on the biology of the immune system as well as the risk for cancer.
URL:http://www.physics.wisc.edu/twap/view.php?id=2741
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