Motor protein tails contain dynamic and context-dependent structural motifs that regulate cargo interactions and motor activation, challenging the view of them as mostly disordered.
Motor protein tails, previously thought to be mostly disordered, contain context-dependent structural motifs that regulate transport.
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Motor protein tails, long considered flexible and disordered linkers that mediate transient cargo interactions, are increasingly recognized as dynamic hubs containing context-dependent structural motifs. Advances in cryo-EM single-particle analysis, flexible refinement tools, and in situ cryo-ET now allow visualization of partially ordered elements within these flexible regions. Recent studies of kinesin reveal that local folding events regulate adaptor binding, cargo recognition, and motor activation, challenging the traditional view of the kinesin tail as mostly disordered. This emerging perspective highlights motor tails as regulatory platforms where intrinsic disorder coexists with hidden structure, reshaping our understanding of transport regulation.
Niu et al. (Wed,) reported a other. Motor protein tails contain dynamic and context-dependent structural motifs that regulate cargo interactions and motor activation, challenging the view of them as mostly disordered.