Key result
The potent inhibitory activity of the Myosin-5a globular tail domain depends on its dimerization, and mutation of two conserved basic residues weakens this inhibition while enhancing activation by melanophilin.
The study reveals that the inhibitory activity of myosin-5a's globular tail domain depends on its dimerization, providing insights into the regulation of its motor function.
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Should not change practice; leaves open extension of myosin-5a dimerization mechanisms to human models.
Zhang et al. (2016) studied this question. GTD dimerization and mutation (R1490A/K1491A) vs. Wild type Myo5a was evaluated on ATPase activity and binding affinity (Kd). The potent inhibitory activity of the Myosin-5a globular tail domain depends on its dimerization, and mutation of two conserved basic residues weakens this inhibition while enhancing activation by melanophilin.
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