BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
X-WR-CALNAME:Biophysics Colloquium with Lukas Tamm
X-WR-TIMEZONE:Eastern Time (US & Canada)
BEGIN:VEVENT
DTSTAMP:20260905T211422Z
UID:tag:localist.com\,2008:EventInstance_2247942
DTSTART:20161130T210000Z
DTEND:20161130T220000Z
DESCRIPTION:Lukas Tamm\, School of Medicine\, University of Virginia\n\nHos
 t: Susan Daniel & Gerald Feigenson\n\nMultiple roles of cholesterol in cel
 l entry of HIV and Ebola viruses and exocytotic fusion pore formation\n\nC
 holesterol plays complex roles in modulating the dynamical structure of ce
 ll membranes. For example\, viral envelope proteins such as influenza HA\,
  HIV gp120/gp41\, and Ebola GP1/GP2 utilize cholesterol-rich lipid domains
  to bud off cell membranes and to enter cells by membrane fusion. Interest
 ingly\, we found recently that the perimeters and not the platforms of cho
 lesterol-rich lipid domains (“rafts”) constitute the main sites of HIV
  entry by membrane fusion. These viruses take advantage of “line tension
 ” that exists at raft boundaries for cell entry. Similarly\, membrane-in
 tegral SNARE proteins that are responsible for rapid membrane fusion in sy
 naptic exocytosis redistribute in the membranes in a fashion that is tight
 ly regulated by cholesterol and the signaling lipid PIP2.  Single particle
  fusion assays show that the progression of an initial hemi-fusion interme
 diate to an open exocytotic fusion pore is strongly promoted by cholestero
 l.\n\n \n\nReferences:\n\nYang ST\, Kreutzberger AJ\, Lee J\, Kiessling V\
 , (2016) The role of cholesterol in membrane fusion. Chem Phys Lipids 199:
 136-143.Kreutzberger AJB\, Kiessling V\, and Tamm LK (2015) High cholester
 ol obviates a prolonged hemifusion intermediate in fast SNARE-mediated mem
 brane fusion. Biophys J 109:1-11.Simmons JA\, White JM\, and Tamm LK (2015
 ) HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich li
 pid domains. Nature Chem Biol 11:424-431.Yang ST\, Kiessling V\, Tamm LK (
 2016) Line tension at lipid phase boundaries as a driving force for HIV fu
 sion peptide-mediated fusion. Nat Commun 7:11401.poster
GEO:42.449741;-76.481209
LOCATION:Clark Hall\, 700
SUMMARY:Biophysics Colloquium with Lukas Tamm
URL;VALUE=URI:https://events.cornell.edu/event/biophysics_colloquium_with_l
 ukas_tamm
CATEGORIES:Seminar
END:VEVENT
END:VCALENDAR