BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VTIMEZONE
TZID:Europe/Vienna
BEGIN:DAYLIGHT
DTSTART:20170326T030000
TZOFFSETFROM:+0100
TZOFFSETTO:+0200
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=3
TZNAME:CEST
END:DAYLIGHT
BEGIN:STANDARD
DTSTART:20161030T020000
TZOFFSETFROM:+0200
TZOFFSETTO:+0100
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=10
TZNAME:CET
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTAMP:20260429T013931Z
UID:58789ae0d5262850517130@ist.ac.at
DTSTART:20170123T150000
DTEND:20170123T163000
DESCRIPTION:Speaker: Daniel Van Damme\nhosted by Eva Benkova\nAbstract: The
  plant plasma membrane (PM) contains a wide range of receptors\, channels 
 and other integral membrane proteins that control nutrient uptake and medi
 ate communication of the cell with the outside world. Modulation of signal
 ling pathways starting from the PM requires control over the PM proteome. 
 While anterograde secretory pathways deposit PM proteins\, their removal d
 epends on retrograde transport by endocytosis\, in which PM material and e
 xtracellular ligands are predominantly internalized using coated vesicles.
  Clathrin-mediated endocytosis (CME)\, defined by the involvement of the s
 caffold protein clathrin to form the cage around the invaginating membrane
 \, is the best characterized endocytic pathway in eukaryotes. Initiation o
 f CME relies on adaptor proteins\, which precisely select the cargo to be 
 internalized\, recruit the clathrin cage and facilitate membrane curvature
 . The identification of the TPLATE complex (TPC) as a novel adaptor comple
 x regulating CME in plants challenges the general belief that the mechanis
 m of CME is highly conserved in eukaryotes. The TPC consists out of eight 
 proteins for which no obvious homologs could be identified in animal or ye
 ast genomes. An extensive structural homology-based search did however ide
 ntify a similar hexameric complex (TSET) in the slime mold Dictyostelium. 
 The TPC/TSET complex is claimed to represent an evolutionary ancient adapt
 or complex which is lost completely in the lineage leading to animal and f
 ungal cells. Structural modeling and identification of specific protein do
 mains led to a theoretical model of the TPC. This model shows that the TPC
  shares many features with the evolutionary conserved AP-2 and COPI comple
 xes\, but also has distinct differences. Subunit co-interaction assays in 
 yeast and N. benthamiana confirmed the structural predictions of the model
  and revealed that the TPC is likely a hexameric core complex which associ
 ates with its two peripheral subunits\, forming the full octameric TPC at 
 the PM. To ultimately reveal the order of recruitment of the various playe
 rs at the PM during CME and to analyze the immediate effects on retrograde
  transport by inactivating the TPC\, novel tools are being developed.
LOCATION:Mondi Seminar Room 3\, Central Building\, ISTA
ORGANIZER:hsemerad@ist.ac.at
SUMMARY:Daniel Van Damme: Towards structural insight into the endocytic TPL
 ATE Adaptor Complex
URL:https://talks-calendar.ista.ac.at/events/262
END:VEVENT
END:VCALENDAR