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Journal of Cell Science 114, 1981-1998 (2001)
© 2001 The Company of Biologists Limited


COMMENTARY

Myosin learns to walk

Amit Mehta

Howard Hughes Medical Institute and Laboratory of Sensory Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA

(e-mail: mehtaa{at}rockvax.rockefeller.edu)

Recent experiments, drawing upon single-molecule, solution kinetic and structural techniques, have clarified our mechanistic understanding of class V myosins. The findings of the past two years can be summarized as follows: (1) Myosin V is a highly efficient processive motor, surpassing even conventional kinesin in the distance that individual molecules can traverse. (2) The kinetic scheme underlying ATP turnover resembles those of myosins I and II but with rate constants tuned to favor strong binding to actin. ADP release precedes dissociation from actin and is rate-limiting in the cycle. (3) Myosin V walks in strides averaging ~36 nm, the long pitch pseudo-repeat of the actin helix, each step coupled to a single ATP hydrolysis. Such a unitary displacement, the largest molecular step size measured to date, is required for a processive myosin motor to follow a linear trajectory along a helical actin track.

Key words: Myosin V, Single-molecule mechanics, Solution kinetics, Load-dependent kinetics, Structure, Molecular models


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© The Company of Biologists Ltd 2001