SSBD:database

Project ID

191-Shima-KIF5Cmove

Title

KIF5C running on various states of microtubules

Description

Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide- free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second- harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.

Release Date

2024-12-14

Update Date

-

License

CC BY

Version

-

Method Summary

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Paper DOI

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Paper URL

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Kind

Total

84 files / 2.4 GB

Image datasets

zipped 6 files / 742.0 MB, raw image 75 files / 1.6 GB, total 81 files / 2.4 GB

Quantitative datasets

zipped 0 files / 0 bytes, raw bdml 0 files / 0 bytes, total 0 files / 0 bytes

Organism

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Strain

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Cell line

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Biological Process

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Cellular Component

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Medical Subject Headings

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Method involved in biological imaging