Mechanism of tail-mediated inhibition of kinesin activities studied using synthetic peptides

Hisashi Yonekura, Akiko Nomura, Hitomi Ozawa, Yoshiro Tatsu, Noboru Yumoto, Taro Q.P. Uyeda*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


We used a truncated form of human conventional kinesin (K560) and a set of synthetic tail-derived peptides to investigate the mechanism by which the kinesin tail domain inhibits the protein's ATPase and motor activities. A peptide that spans residues 904-933 (C3) exhibited the strongest inhibitory effect on steady-state motility and ATPase activity. This inhibition reflected diminished binding of the ADP-bound kinesin head to the microtubule. Although peptide C3 bound to both K560 and microtubules, gliding assays using subtilisin-treated microtubules suggested that the binding to the microtubule contributes only little to the inhibition if there is sufficient affinity between the peptide and kinesin. We suggest that tail-mediated inhibition of kinesin activity is mainly the product of allosteric inhibition induced by the intramolecular binding of the kinesin tail domain to the motor domain, but simultaneous binding of the tail to the microtubule also may exert a minor effect.

Original languageEnglish
Pages (from-to)420-427
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2006 May 5
Externally publishedYes


  • ATPase
  • Autoinhibition
  • In vitro motility
  • Kinesin
  • Microtubule
  • Peptide

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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