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TitleTension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.
Journal, issue, pagesJ Cell Biol, Vol. 224, Issue 7, Year 2025
Publish dateJul 7, 2025
AuthorsTsukasa Makino / Ryo Kanada / Teppei Mori / Ken-Ichi Miyazono / Yuta Komori / Haruaki Yanagisawa / Shoji Takada / Masaru Tanokura / Masahide Kikkawa / Michio Tomishige /
PubMed AbstractKinesin-1 walks along microtubules by alternating ATP hydrolysis and movement of its two motor domains ("head"). The detached head preferentially binds to the forward tubulin-binding site after ATP ...Kinesin-1 walks along microtubules by alternating ATP hydrolysis and movement of its two motor domains ("head"). The detached head preferentially binds to the forward tubulin-binding site after ATP binds to the microtubule-bound head, but the mechanism preventing premature microtubule binding while the partner head awaits ATP remains unknown. Here, we examined the role of the neck linker, the segment connecting two heads, in this mechanism. Structural analyses of the nucleotide-free head revealed a bulge just ahead of the neck linker's base, creating an asymmetric constraint on its mobility. While the neck linker can stretch freely backward, it must navigate around this bulge to extend forward. We hypothesized that increased neck linker tension suppresses premature binding of the tethered head, which was supported by molecular dynamics simulations and single-molecule fluorescence assays. These findings demonstrate a tension-dependent allosteric mechanism that coordinates the movement of two heads, where neck linker tension modulates the allosteric conformational changes rather than directly affecting the nucleotide state.
External linksJ Cell Biol / PubMed:40298806 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.4 - 3.48 Å
Structure data

62874

9l7m

EMDB-62874, PDB-9l7m:
Nucleotide-free kinesin-1 motor domain bound to the microtubule
Method: EM (single particle) / Resolution: 3.48 Å

PDB-9l6k:
Crystal structure of nucleotide-free human kinesin-1 motor domain (G234V mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-9l78:
Crystal structure of nucleotide-free human kinesin-1 motor domain (G234A mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

PDB-9l7e:
Crystal structure of human kinesin-1 motor domain (G234A mutant) in complex with ADP
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • sus scrofa (pig)
  • homo sapiens (human)
KeywordsMOTOR PROTEIN / kinesin / Microtubule

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