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UID:DSC-21321
DTSTART;TZID=Europe/Berlin:20241001T100000
SEQUENCE:1727761226
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20241001T110000
URL:https://www.dresden-science-calendar.de/calendar/de/detail/21321
LOCATION:MPI-CBG\, Pfotenhauerstraße 10801307 Dresden
SUMMARY:Hellmich: Multilayered regulatory networks in the intrinsically dis
 ordered regions  of TRP ion channels
CLASS:PUBLIC
DESCRIPTION:Speaker: Ute A. Hellmich\nInstitute of Speaker: Institute of Or
 ganic Chemistry and Macromolecular Chemistry\, Friedrich Schiller Universi
 ty Jena\nTopics:\n\n Location:\n  Name: MPI-CBG (MPI-CBG: Auditorium Small
 )\n  Street: Pfotenhauerstraße 108\n  City: 01307 Dresden\n  Phone: +49 3
 51 210-0\n  Fax: +49 351 210-2000\nDescription: Intrinsically disordered r
 egions (IDRs) are essential for membrane receptor regulation but often rem
 ain unresolved in structural studies. The members of the Transient Recepto
 r Potential (TRP) channel superfamily of ion channels are characterized by
  large N- and C-terminal IDRs that mediate intra- and intermolecular conta
 cts with other proteins and the lipid bilayer1. TRP channels play central 
 roles in almost every (patho)physiological process\, including thermo- and
  osmosensation\, nociception and infectious diseases2. A molecular underst
 anding of the polymodality of TRP channel regulation is thus crucial for a
  fundamental understanding of sensory perception and cellular responses to
  diverse stimuli. We hypothesize that the IDRs harbor regulatory elements 
 that allow TRP channels to meaningfully integrate diverse signaling inputs
 .  We recently generated the first full-length structural model of a TRP c
 hannel\, TRP Vanilloid 4\, that takes the dimensions of the IDR and its me
 mbrane-interactions into account3. Intriguingly\, deletion of the channel
 ’s N-terminal IDR\, consisting of ~150 amino acids\, renders TRPV4 unres
 ponsive to osmotic stimuli\, while distinct IDR regions enhance or subdue 
 channel function. Together\, these regulatory elements in the IDR modulate
  channel responses in a hierarchical\, lipid-dependent manner. To enhance 
 our understanding of TRP channel regulation by its large IDR\, we also inc
 orporated small molecules\, proteins and disease mutations4 into our funct
 ional model of TRPV4. Furthermore\, by exploring the structural dynamics a
 nd functional roles of the IDRs in other TRP channels\, we find that multi
 layered signal integration by the IDRs is a widespread phenomenon in this 
 important protein family. Accordingly\, to understand TRP channel function
 \, their often extensive IDRs cannot be ignored.  Our work shows that “I
 DR cartography”\, i.e.\, mapping structural and functional properties on
 to distinct IDR regions through an integrated structural biology approach\
 , sheds light on the complex regulation of membrane receptors through thei
 r hitherto mostly neglected regions and provides a framework for signal in
 tegration on the molecular level.
DTSTAMP:20260710T165052Z
CREATED:20240925T144904Z
LAST-MODIFIED:20241001T054026Z
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