Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.

ABSTRACT: Contractile force transduction by myosin II derives from its assembly into bipolar filaments. The coiled-coil tail domain of the myosin II heavy chain mediates filament assembly, although the mechanism is poorly understood. Tail domains contain an alternating electrostatic repeat, yet only a small region of the tail (termed the "assembly domain") is typically required for assembly. Using computational analysis, mutagenesis, and electron microscopy we discovered that the assembly domain does not function through self-interaction as previously thought. Rather, the assembly domain acts as a unique, positively charged interaction surface that can stably contact multiple complementary, negatively charged surfaces in the upstream tail domain. The relative affinities of the assembly domain to eac

SUBMITTER: Ricketson D 

PROVIDER: S-EPMC3000310 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature