Myosin light chain kinase (210 kDa) is a potential cytoskeleton integrator through its unique N-terminal domain.

Recently discovered 210-kDa myosin light chain kinase (MLCK-210) is identical to 108-130 kDa MLCK, the principal regulator of the myosin II molecular motor, except for the presence of a unique amino terminal extension. Our in vitro experiments and transfected cell studies demonstrate that the N-terminal half of MLCK-210 unique tail domain has novel microfilament and microtubule binding activity. Consistent with this activity, the MLCK-210 domain codistributes with microfilaments and microtubules in cultured cells and with soluble tubulin in nocodazole-treated cells.