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Updated: Apr 15, 2026

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
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Kinesin-1 conformational dynamics are controlled by a cargo-sensitive TPR switch.

Shivam Shukla1,2, Jessica A Cross1,2,3, Monika Kish4,5

  • 1School of Biochemistry and Biomedical Sciences, University of Bristol, Biomedical Sciences Building, University Walk, Bristol, United Kingdom.

Elife
|April 14, 2026
PubMed
Summary
This summary is machine-generated.

Kinesin-1 activation involves cargo-adaptor proteins dislocating the KLC-TPR shoulder. This structural change frees motor domains, linking cargo binding to motor dynamics for intracellular transport.

Keywords:
cell biologycytoskeletonhumankinesinmolecular motormouserat

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Kinesin-1 is a motor protein complex essential for intracellular transport.
  • It exists in a compact, autoinhibited state, activated by cargo-adaptor proteins.
  • Short linear motifs (SLiMs) on adaptors interact with Kinesin Light Chain (KLC) tetratricopeptide repeat (TPR) domains.

Purpose of the Study:

  • To elucidate the mechanism coupling SLiM recognition to activation-induced conformational changes in Kinesin-1.
  • To investigate the structural consequences of SLiM binding to KLC-TPR domains within the holoenzyme.

Main Methods:

  • Protein design
  • Computational modeling
  • Biophysical analysis
  • Electron microscopy

Main Results:

  • Coiled coil 1 (CC1) of Kinesin Heavy Chain (KHC) docks KLC-TPR domains, forming an autoinhibited 'shoulder'.
  • Disrupting this interaction or SLiM binding dislocates the TPR shoulder, releasing motor domains.
  • This promotes the transition from closed, inactive states to open states, facilitating microtubule binding.

Conclusions:

  • Cargo-mediated dislocation of the TPR shoulder is a critical initial step in Kinesin-1 activation.
  • This mechanism allosterically links cargo binding to motor domain dynamics and microtubule association.
  • The findings reveal how cargo adaptors control Kinesin-1 activity for transport.