Motor protein tails: Hidden order within disorder

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.