Dynein and Dynactin Leverage Their Bivalent Character to Form a High-Affinity Interaction (original) (raw)
Figure 9
Proposed mechanism of dynein-dynactin binding.
Based on the refinement of the dynein-dynactin interaction and the physical characterization of the individual fragments, we propose that the N-terminus of the dynein IC is disordered in the in the absence of dynactin. Further, based on recent data from our lab and others we propose that the dynein LCs affect the N-termini by reducing and/or orienting the N-termini of the IC to optimally bind to dynactin. Taken together, we suggest the following model: A. The N-terminus of the intermediate chain exists in a disordered state. B. Upon IC binding to the light chains the radius of gyration of the disordered region is reduced. C. The N-termini of the IC bind to p150Glued CC1B located in the shoulder.