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SUMMARY:How end binding proteins recognise growing microtubule ends: from 
 molecular structure to network functioning - Thomas Surrey\, Cancer Resear
 ch UK\, London Research Institute
DTSTART:20120426T151500Z
DTEND:20120426T170000Z
UID:TALK37283@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The microtubule cytoskeleton performs essential mechano-chemic
 al tasks in eukaryotic cells. Growing microtubule ends serve as transient 
 binding platforms for several proteins that regulate microtubule dynamics 
 and interactions with cellular substructures. End Binding proteins (EBs) r
 ecruit most of these proteins. They autonomously recognize an extended reg
 ion at growing microtubule ends with unknown structural characteristics. U
 sing in vitro reconstitutions in combination with fluorescence microscopy 
 we dissect the interplay between EBs and their recruited proteins. Using c
 ryo-electron microscopy and subnanometer single particle reconstruction an
 d fluorescence imaging\, we construct a pseudo-atomic model of how EBs bin
 d to the end region of growing microtubules. They bridge protofilaments ex
 cept at the microtubule seam. By binding close to the exchangeable GTP bin
 ding site of tubulin\, they are ideally positioned to sense the microtubul
 e’s nucleotide state. Strikingly\, the microtubule end region that is re
 cognized by EBs is also a stabilizing structural cap protecting the microt
 ubule from depolymerisation. This reveals a common structural link between
  two important biological phenomena\, microtubule dynamic instability and 
 end tracking.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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