BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VTIMEZONE
TZID:Europe/Vienna
BEGIN:DAYLIGHT
DTSTART:20250330T030000
TZOFFSETFROM:+0100
TZOFFSETTO:+0200
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=3
TZNAME:CEST
END:DAYLIGHT
BEGIN:STANDARD
DTSTART:20251026T020000
TZOFFSETFROM:+0200
TZOFFSETTO:+0100
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=10
TZNAME:CET
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTAMP:20260424T143352Z
UID:1750766400@ist.ac.at
DTSTART:20250624T140000
DTEND:20250624T150000
DESCRIPTION:Speaker: Hanna Schön\nhosted by Beatriz Vicoso\nAbstract: This
  thesis elucidates functions for two previously uncharacterized proteins\,
  suppressor of tumorigenicity 7 (SUTU-7) and macoilin (MACO-1). Mutants de
 fective in these proteins were identified in a forward genetic screen for 
 animals that lost the ability to aggregate\, a behavior linked to oxygen s
 ensing. Aggregation is controlled by a hub-and-spoke circuit that consists
  of the RMG hub interneurons and an array of sensory neurons linked to RMG
  via electrical and/or chemical synapses. SUTU-7 is a membrane protein of 
 unknown function conserved across metazoa. Mutants of sutu-7 are healthy b
 ut have the signature behavioral phenotypes associated with low activity i
 n the RMG circuit: defects in escape from 21% O2\, elevated escape from CO
 2\, and robust escape from hypoxia. We found that SUTU-7 shows a broad and
  predominantly neuronal expression pattern and resides in the endoplasmic 
 reticulum (ER). SUTU-7 forms a complex with MACO-1\, which recruits the de
 adenylation complex CCR4-Not to the ER. Our data suggest that SUTU-7 inter
 acts with membrane proteins\, including GPCRs\, as they are made in the ER
 . The O2 response defects of sutu-7 mutants reflect stabilization of mRNA 
 encoding the GPCR NPR-1\, which inhibits the RMG interneurons. A series of
  qPCR experiments suggest that SUTU-7 destabilizes mRNAs encoding most C. 
 elegans GPCRs. Tunicamycin treatment\, which disrupts protein folding by i
 nhibiting N-linked glycosylation\, broadens the number of mRNAs negatively
  regulated by SUTU-7. Our data suggest SUTU-7/MACO-1 form an ER quality co
 ntrol complex that destabilizes mRNAs encoding wild type GPCRs\, likely in
  response to aberrant receptor biogenesis.
LOCATION:Sunstone Bldg / Ground floor / Big Seminar Room A (I23.EG.102) and
  Zoom\, ISTA
ORGANIZER:
SUMMARY:Hanna Schön: Thesis Defense: The ER complex SUTU-7/MACO-1 regulate
 s the fate of mRNAs encoding GPCRs 
URL:https://talks-calendar.ista.ac.at/events/5855
END:VEVENT
END:VCALENDAR