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- W2007624488 abstract "Myosin-Is are widely expressed molecular motors that comprise the second largest myosin family in vertebrates with eight isoforms. Myosin-Is participate in a host of cellular processes including vesicular trafficking, membrane dynamics, and nuclear transcription. The question thus arises, how can these motors with similar biochemical properties give rise to such diversity of function? The answer appears to lie in the biochemical and mechanical diversity of the isoforms. Our biophysical studies demonstrate that Myo1b is exquisitely sensitive to tension, where forces >0.5 pN cause the motor to transform from a low duty ratio motor with attachment lifetimes 50 s. Our studies also reveal that the isoform Myo1c has a very different response to force despite its similar unloaded kinetics to Myo1b. Myo1c is far less sensitive to force than Myo1b, enabling it to power motility over a range of forces, consistent with it serving a role as a transporter rather than as a tension-sensitive anchor. To better understand the molecular basis for these differences in force sensing, we have determined the crystal structure of Myo1b's motor domain and first IQ-motif with bound calmodulin. The structure reveals novel interactions between the light-chain binding domain and the N-terminus of the motor domain, a region that shows substantial sequence variability among myosin-I isoforms. We propose that these interactions facilitate communication between the lever arm and the ATP binding site, modulating the chemomechanical properties of the motor. Supported by the NIH (GM057247)." @default.
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- W2007624488 date "2014-01-01" @default.
- W2007624488 modified "2023-09-28" @default.
- W2007624488 title "Structural, Mechanical, and Biochemical Insights into the Mechanism of Myosin Force Sensing" @default.
- W2007624488 doi "https://doi.org/10.1016/j.bpj.2013.11.101" @default.
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