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SUMMARY:Antagonistic motor protein dynamics in contractile ring structures
  - Adriana Dawes (Ohio State)
DTSTART:20200312T130000Z
DTEND:20200312T140000Z
UID:TALK140758@talks.cam.ac.uk
CONTACT:George Fortune
DESCRIPTION:Ring-shaped contractile structures play important roles in bio
 logical processes including wound healing and cell division. Many of these
  contractile structures rely on motor proteins called myosins for constric
 tion. We investigate force generation by the Type II myosins NMY-1 and NMY
 -2 in ring channels\, contractile structures in developing oocytes of the 
 nematode worm C. elegans\, as our model system. By exploiting the ring cha
 nnel's circular geometry\, we derive a second order ODE to describe the ev
 olution of the radius of the ring channel. By comparing our model predicti
 ons to experimental depletion of NMY-1 and NMY-2\, we show that these myos
 ins act antagonistically to each other\, with NMY-1 exerting force orthogo
 nally and NMY-2 exerting force tangentially to the ring channel opening. S
 tochastic simulations are currently being used to determine how NMY-1 and 
 NMY-2 may be producing these antagonistic forces\, with new tools from top
 ological data analysis identifying persistent ring-like structures in the 
 simulation data.
LOCATION:MR11\, Centre for Mathematical Sciences\, Wilberforce Road\, Camb
 ridge
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