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Related Experiment Video

Updated: Feb 7, 2026

Assembly and Characterization of Polyelectrolyte Complex Micelles

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

Structural characterization of a minimal KLC2/Nup358/BicD2 complex.

Crystal R Noell, Sozanne R Solmaz

Biorxiv : the Preprint Server for Biology

|February 6, 2026

Summary

This summary is machine-generated.

Cellular transport relies on multi-motor protein complexes. This study reveals how Kinesin-1 light chain 2 (KLC2) and Bicaudal D2 (BicD2) cooperatively bind Nup358, influencing motor recruitment for nuclear positioning.

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Last Updated: Feb 7, 2026

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Area of Science:

Cellular biology
Molecular motors
Protein structure and dynamics

Background:

Cellular transport along microtubules involves multi-motor protein complexes.
Nuclear pore protein Nup358 interacts with Bicaudal D2 (BicD2) to recruit dynein and kinesin-1 motors for nuclear positioning.
Regulation of motor recruitment by BicD2-Nup358 interactions is not fully understood.

Purpose of the Study:

To characterize the structure of a minimal complex of kinesin-1 light chain 2 (KLC2), Nup358, and BicD2.
To elucidate the mechanism of motor recruitment regulation by BicD2 and Nup358.

Main Methods:

Cryo-electron microscopy (cryo-EM) to determine complex structure.
Small-angle X-ray scattering (SAXS) to analyze complex shape and stoichiometry.
Biochemical assays to study protein interactions and oligomerization.

Main Results:

KLC2/Nup358 forms a rod-like structure that thickens upon BicD2 binding.
BicD2 binding shifts the KLC2/Nup358/BicD2 complex towards a 2:2:2 stoichiometry, promoting dimerization.
Nup358/KLC2 interaction also favors a 2:2:2 stoichiometry.

Conclusions:

KLC2 and BicD2 are cooperatively recruited to Nup358.
Cooperative binding is potentially mediated by modulation of the complex's oligomeric state.
Understanding this mechanism provides insights into nuclear positioning and brain development pathways.