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Biased Brownian Motion of KIF1A and the Role of Tubulin’s C-Terminal Tail Studied by Molecular Dynamics Simulation

Authors
  • mizuhara, yukinobu
  • takano, mitsunori
Publication Date
Feb 04, 2021
Identifiers
DOI: 10.3390/ijms22041547
OAI: oai:mdpi.com:/1422-0067/22/4/1547/
Source
MDPI
Keywords
Language
English
License
Green
External links

Abstract

KIF1A is a kinesin family protein that moves over a long distance along the microtubule (MT) to transport synaptic vesicle precursors in neurons. A single KIF1A molecule can move toward the plus-end of MT in the monomeric form, exhibiting the characteristics of biased Brownian motion. However, how the bias is generated in the Brownian motion of KIF1A has not yet been firmly established. To elucidate this, we conducted a set of molecular dynamics simulations and observed the binding of KIF1A to MT. We found that KIF1A exhibits biased Brownian motion along MT as it binds to MT. Furthermore, we show that the bias toward the plus-end is generated by the ratchet-like energy landscape for the KIF1A-MT interaction, in which the electrostatic interaction and the negatively-charged C-terminal tail (CTT) of tubulin play an essential role. The relevance to the post-translational modifications of CTT is also discussed.

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