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• W2028764383 abstract "The motor head of kinesin carries out microtubule binding, ATP hydrolysis, and force generation. Despite a high level of sequence and structural conservation, subtle variations in subdomains of the motor head determine family-specific properties. In particular, both Kinesin-1 (Kin-1) and Kinesin-5 (Kin-5) walk processively to the microtubule plus-end, yet show distinct motility characteristics suitable for their functions. We studied chimeric Kin-1/Kin-5 constructs with a combination of single molecule motility assays and molecular dynamics simulations to demonstrate that Kin-5 possesses a force-generating element similar to Kin-1, i.e., the cover-neck bundle. Furthermore, the Kin-5 neck linker makes additional contacts with the core of the motor head via loop L13, which putatively compensates for the shorter cover-neck bundle of Kin-5. Our results indicate that Kin-1 is mechanically optimized for individual cargo transport, whereas Kin-5 does not necessarily maximize its mechanical performance. Its biochemical rates and enhanced force sensitivity may instead be beneficial for operation in a group of motors. Such variations in subdomains would be a strategy for achieving diversity in motility with the conserved motor head." @default.
• W2028764383 created "2016-06-24" @default.
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• W2028764383 date "2013-05-01" @default.
• W2028764383 modified "2023-10-07" @default.
• W2028764383 title "Modular Aspects of Kinesin Force Generation Machinery" @default.
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• W2028764383 doi "https://doi.org/10.1016/j.bpj.2013.03.051" @default.
• W2028764383 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3647194" @default.
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