She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain.
Cytoplasmic dynein is an enormous minus end-directed microtubule motor. Rather than existing as bare tracks, microtubules are bound by numerous microtubule-associated proteins (MAPs) that have the capacity to affect various cellular functions, including motor-mediated transport. One such MAP is She1, a dynein effector that polarizes dynein-mediated spindle movements in budding ... yeast. Here, we characterize the molecular basis by which She1 affects dynein, providing the first such insight into which a MAP can modulate motor motility. We find that She1 affects the ATPase rate, microtubule-binding affinity, and stepping behavior of dynein, and that microtubule binding by She1 is required for its effects on dynein motility. Moreover, we find that She1 directly contacts the microtubule-binding domain of dynein, and that their interaction is sensitive to the nucleotide-bound state of the motor. Our data support a model in which simultaneous interactions between the microtubule and dynein enables She1 to directly affect dynein motility.
Mesh Terms:
Amino Acid Sequence, Dyneins, Microscopy, Fluorescence, Microtubule-Associated Proteins, Microtubules, Models, Biological, Models, Molecular, Molecular Motor Proteins, Myosin Heavy Chains, Myosin Type V, Protein Binding, Protein Domains, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Amino Acid Sequence, Dyneins, Microscopy, Fluorescence, Microtubule-Associated Proteins, Microtubules, Models, Biological, Models, Molecular, Molecular Motor Proteins, Myosin Heavy Chains, Myosin Type V, Protein Binding, Protein Domains, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Nat Commun
Date: Dec. 15, 2016
PubMed ID: 29247176
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