How elasticity and entropy drive self-organization of
filament crosslinking proteins, in and out of equilibrium
Glen Hocky, NYU
The actin cytoskeleton is a crucial biological system that
plays a role in cell division, motion, and internal transport.
The main component is filamentous actin, a semiflexible polymer
formed of proteins called actin monomer.
For a cell to regulate
and accomplish the tasks of the cytoskeleton, actin
polymers are organized into structures by actin binding
proteins. Crosslinking proteins join actin into a network with
structural rigidity, and form tight bundles that are more stiff
than single filaments. Different crosslinkers perform
diverse functions in cells, and their spatial localization is
crucial for those functions.
In this talk, I will first describe a general simulation
framework we have developed for studying the structure and
mechanics of active crosslinked filament networks, such as the
actin cytokeleton. I will then describe how we have used this
simulation framework in conjunction with theory and Monte Carlo
simulations of a lattice model to study the physical driving
forces underlying a newly mechanism by which different actin
crosslinking proteins can sort themselves.