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SUMMARY:PP2A-B55 inhibitors Arpp19 and ENSA define the cell cycle program 
 by controlling the temporal pattern of protein phosphorylation - Dr Anna C
 astro\, CRBM-CNRS\, Montpellier 
DTSTART:20210311T160000Z
DTEND:20210311T170000Z
UID:TALK150574@talks.cam.ac.uk
CONTACT:Caroline Newnham
DESCRIPTION:Cell cycle progression is controlled by the sequential and ord
 ered phosphorylation of cell phase specific substrates. This phosphorylati
 on is the result of the balance between cyclin/cdk kinases and their count
 eracting phosphatases. PP2A-B55 is one of these phosphatases. During the c
 ell cycle\, the activity of PP2A-B55 is regulated by the Greatwall (Gwl) k
 inase and their substrates Arpp19 and ENSA. The phosphorylation of Arpp19 
 and ENSA by Gwl promotes their binding to PP2A-B55 and the inhibition of t
 his phosphatase. How this binding results in the inhibition of this enzyme
  is not known. Moreover\, how this pathway can induce the correct temporal
  and spatial inactivation of PP2A-B55 required for the ordered dephosphory
 lation of the cell cycle substrates is elusive. Using Xenopus egg extract 
 model\, we shed light in the molecular mechanisms defining the PP2A-B55 in
 hibitory activity of Arpp19 and ENSA. Moreover\, we also identified a diff
 erential role of the two PP2A-B55 inhibitors. Notably\, our “in cellulo
 ” and “in vivo” data demonstrate that the ENSA protein participates 
 to the correct phosphorylation of S phase substrates while Arpp19 plays an
  essential role to promote the ordered substrate dephosphorylation pattern
  required for a correct mitotic exit.
LOCATION:Zoom meeting
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