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SUMMARY:Tea Club Seminar - Manu Hegde &quot\;How our cells make multi-pass
  membrane proteins&quot\; - Manu Hegde
DTSTART:20220301T123000Z
DTEND:20220301T140000Z
UID:TALK170162@talks.cam.ac.uk
CONTACT:Ben Luisi
DESCRIPTION:\nMammals encode ~5000 integral membrane proteins that need to
  be inserted in a defined topology at the endoplasmic reticulum membrane. 
 The majority of these membrane proteins have multiple transmembrane domain
 s that have to be weaved back and forth across the lipid bilayer and assem
 bled into a functional three-dimensional structure. How such multi-pass me
 mbrane proteins are made correctly is not well understood. My group has be
 en studying the processes of membrane protein targeting\, insertion\, and 
 folding. Starting with very simple model membrane proteins\, we have taken
  a biochemical approach to identify and mechanistically dissect the factor
 s involved in these processes. In this talk\, I will describe our recent e
 fforts at tackling the problem of how multi-pass membrane proteins are mad
 e. Using G-protein coupled receptors (GPCRs) as a particularly important e
 xample\, we have begun to find that the textbook view of how multi-pass pr
 oteins are made is incomplete\, or in some cases\, incorrect. My talk will
  cover our recent discoveries of a new membrane protein insertase that act
 s early during GPCR biogenesis\, a novel type of chaperone that helps duri
 ng membrane protein folding\, and the conceptual insights that have come f
 rom understanding how these factors work.\n
LOCATION:Jean Thomas Lecture theatre\, Sanger Building\, Tennis Court Road
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