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SUMMARY:Role of Gasdermin-D in inflammasome effector mechanisms
DTSTART:20170131T121500
DTSTAMP:20260916T044018Z
UID:fab14edae112bd10cb66fe1be03e7837494ff9a75499c0ae6ec876de
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Petr Broz\,  Focal Area Infection Biology\, Biozentrum\
 , University of Basel\nAbstract:\nPyroptosis is a lytic type of cell death
  that is initiated by inflammatory caspases. These caspases are activated 
 within multi‐protein inflammasome complexes that assemble in response t
 o pathogens and endogenous danger signals. Pyroptotic cell death has been 
 proposed to proceed via the formation of a plasma membrane pore\, but the
  underlying molecular mechanism has remained unclear. Recently\, gasdermin
  D (GSDMD)\, a member of the ill‐characterized gasdermin protein family
 \, was identified as a caspase substrate and an essential mediator of pyro
 ptosis. GSDMD is thus a candidate for pyroptotic pore formation. Here\, 
 we characterize GSDMD function in live cells and in vitro. We show tha
 t the N‐terminal fragment of caspase‐1‐cleaved GSDMDrapidly targets
  the membrane fraction of macrophages and that it induces the formation o
 f a plasma membrane pore. In vitro\, the N‐terminal fragment of caspase
 ‐1‐cleaved recombinant GSDMD tightly binds liposomes and forms large
  permeability pores. Visualization of liposome‐inserted GSDMD at nanom
 eter resolution by cryo‐electron and atomic force microscopy shows circ
 ular pores with variable ring diameters around 20 nm. Overall\, these data
  demonstrate that GSDMD is the direct and final executor of pyroptotic 
 cell death.
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
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