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- W4387700432 abstract "Conventional kinesin-1 is the primary anterograde motor in cells for transporting cellular cargo. While there is a consensus that the C-terminal tail of kinesin-1 inhibits motility, the molecular architecture of a full-length autoinhibited kinesin-1 remains unknown. Here, we combine cross-linking mass spectrometry (XL-MS), electron microscopy (EM), and AlphaFold structure prediction to determine the architecture of the full-length autoinhibited kinesin-1 homodimer [kinesin-1 heavy chain (KHC)] and kinesin-1 heterotetramer [KHC bound to kinesin light chain 1 (KLC1)]. Our integrative analysis shows that kinesin-1 forms a compact, bent conformation through a break in coiled coil 3. Moreover, our XL-MS analysis demonstrates that kinesin light chains stabilize the folded inhibited state rather than inducing a new structural state. Using our structural model, we show that disruption of multiple interactions between the motor, stalk, and tail domains is required to activate the full-length kinesin-1. Our work offers a conceptual framework for understanding how cargo adaptors and microtubule-associated proteins relieve autoinhibition to promote activation." @default.
- W4387700432 created "2023-10-18" @default.
- W4387700432 date "2023-10-17" @default.
- W4387700432 modified "2023-10-18" @default.
- W4387700432 title "Reviewer #1 (Public Review): Autoinhibited kinesin-1 adopts a hierarchical folding pattern" @default.
- W4387700432 doi "https://doi.org/10.7554/elife.86776.2.sa0" @default.
- W4387700432 hasPublicationYear "2023" @default.
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