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SUMMARY:NLRP1 inflammasome Activation
DTSTART:20210323T161500
DTEND:20210323T171500
DTSTAMP:20260407T004000Z
UID:a5103ba2e6f49ba89e46944a6be346b503e97a57041aa26e6dde1388
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr. Daniel Bachovchin is an Assistant Professor in the Chemica
 l Biology Program at the Sloan Kettering Institute\, Memorial Sloan Ketter
 ing Cancer Center. His lab uses chemical and cell biology approaches to 
 study proteins and pathways involved in innate immunity\, in particular in
 flammasomes. Dr. Bachovchin received his Ph.D. in 2011 from The Scripps Re
 search Institute under the guidance of Dr. Benjamin F. Cravatt.  From 201
 1-2015\, Dr. Bachovchin was a postdoctoral fellow in Dr. Todd Golub’s la
 boratory at The Broad Institute.       \nIntracellular pathogens and d
 anger signals trigger the formation of inflammasomes\, which activate infl
 ammatory caspases and induce pyroptosis. The anthrax lethal factor metallo
 protease and small-molecule inhibitors of the serine proteases DPP8/9 both
  activate the NLRP1 inflammasome.\n\nWe recently discovered lethal factor 
 lethal factor directly cleaves NLRP1\, triggering the N-end rule-mediated 
 degradation of the NLRP1B N-terminus and freeing the NLRP1 C-terminus to a
 ctivate caspase-1.\n\nWe found that DPP8/9 inhibitors also induce proteaso
 mal degradation of the NLRP1 N-terminus\, but not via the N-end rule pathw
 ay. In order to elucidate the mechanism of DPP8/9 inhibitor-induced pyropt
 osis\, we developed and applied a new chemical strategy for protease subst
 rate profiling called CHOPS.\n\nUsing CHOPS\, we found that DPP8/9 cleave 
 small peptides but not globular proteins. We anticipate that future studie
 s will reveal how DPP8/9 protease activity on these peptides restrains NLR
 P1 and the immune system.\n\n\n\n\n 
LOCATION:https://epfl.zoom.us/j/85636008530
STATUS:CONFIRMED
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