Location and mode of myosin binding of the Dynein Light Chain
A 10 kD dynein light chain (DLC) has been previously shown to bind to the tail of myosin Va (myo5a). It is assumed that DLC functions as a cargo-binding and/or regulatory subunit of both motor proteins.
NMR spectroscopy together with molecular docking simulations suggests that a short synthetic peptide of DBD binds to the surface grooves on DLC2, similarly to other known binding partners of DLCs. We hypothesize that DLC2 brings together the two DBDs of the myoVa heavy chains in an asymmetric manner, leaving one of the binding sites of the DLC2 dimer free to interact with a cargo or regulatory proteins.