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DTSTART:19810329T030000
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UID:DSC-23054
DTSTART;TZID=Europe/Berlin:20261105T000000
SEQUENCE:1790314767
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20261105T000500
URL:https://dresden-science-calendar.org/calendar/en/detail/23054
LOCATION:MPI-CBG\, Pfotenhauerstraße 10801307 Dresden
SUMMARY:Gavin: The molecular machines responsible for organizing lipidomes
CLASS:PUBLIC
DESCRIPTION:Speaker: Anne-Claude Gavin\nInstitute of Speaker: University of
  Geneva\, Switzerland\nTopics:\n\n Location:\n  Name: MPI-CBG (MPI-CBG CBG
  Large Auditorium)\n  Street: Pfotenhauerstraße 108\n  City: 01307 Dresde
 n\n  Phone: +49 351 210-0\n  Fax: +49 351 210-2000\nDescription: Eukaryoti
 c cells produce thousands of different lipids—collectively known as the 
 lipidome—whose composition is tailored to cellular needs. Lipids are dis
 tributed unevenly throughout biological systems\, where they accumulate lo
 cally\, forming membranes with specific compositions and thereby determini
 ng the identity and functional specialization of organelles. Due to their 
 hydrophobicity\, lipids cannot move freely out of cellular membranes throu
 gh the cell’s aqueous environment and require transporters—lipid trans
 fer proteins\, or LTPs—to carry them. LTPs are soluble molecular machine
 s responsible for transporting lipids\, and they are found in all kingdoms
  of life. They have diverse structures\, but many share a common mode of a
 ction: they extract specific lipids from membrane bilayers and load them i
 nto a hydrophobic pocket\, forming water-soluble protein-lipid complexes t
 hat isolate cargoes from the aqueous phase. In addition to their cargo\, s
 ome LTPs mobilize auxiliary lipids that function as exchange currencies or
  cofactors. They facilitate the uptake or release of the cargo\, which wou
 ld determine the direction of transport and its coupling to metabolism. Ho
 wever\, for most LTPs\, the identity of cargo and auxiliary lipids remains
  unknown. The fundamental biochemistry of LTPs remains poorly understood\,
  limiting our ability to study how they function within cells. Our goal is
  to begin addressing this gap\; I will present a recent systematic analysi
 s of the lipid binding properties of human LTPs and discuss the general pr
 inciples that we have derived from it.
DTSTAMP:20260926T055343Z
CREATED:20260725T053712Z
LAST-MODIFIED:20260925T053927Z
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