University of Cambridge > Talks.cam > DAMTP BioLunch > Antagonistic motor protein dynamics in contractile ring structures

Antagonistic motor protein dynamics in contractile ring structures

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Ring-shaped contractile structures play important roles in biological processes including wound healing and cell division. Many of these contractile structures rely on motor proteins called myosins for constriction. 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 channel’s circular geometry, we derive a second order ODE to describe the evolution of the radius of the ring channel. By comparing our model predictions to experimental depletion of NMY -1 and NMY -2, we show that these myosins act antagonistically to each other, with NMY -1 exerting force orthogonally and NMY -2 exerting force tangentially to the ring channel opening. Stochastic simulations are currently being used to determine how NMY -1 and NMY -2 may be producing these antagonistic forces, with new tools from topological data analysis identifying persistent ring-like structures in the simulation data.

This talk is part of the DAMTP BioLunch series.

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