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Updated: Aug 11, 2025
08:04
Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
Published on: January 26, 2019
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Autoinhibited kinesin-1 adopts a hierarchical folding pattern.
Zhenyu Tan1,2, Yang Yue3, Felipe da Veiga Leprevost4
1Department of Biophysics, University of Michigan.
Biorxiv : the Preprint Server for Biology
|February 7, 2023
Summary
Researchers uncovered the structure of autoinhibited kinesin-1, revealing a compact, bent conformation. Kinesin light chains stabilize this inhibited state, requiring disruption of multiple interactions for activation.
Area of Science:
- Molecular biology
- Cellular transport mechanisms
- Protein structure and dynamics
Background:
- Kinesin-1 is the main motor protein for anterograde transport of cellular cargo.
- The C-terminal tail of kinesin-1 is known to inhibit its motility.
- The precise molecular architecture of the full-length autoinhibited kinesin-1 has remained elusive.
Conclusions:
- The study provides the first structural model of autoinhibited kinesin-1.
- Kinesin light chains are stabilizers, not inducers, of the inhibited state.
- A framework is established for understanding how cargo adaptors and MAPs activate kinesin-1.
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