Interaction of monomeric and dimeric kinesin with microtubules

M. Thormählen, A. Marx, S. A. Müller, Y. H. Song, E. M. Mandelkow, U. Aebi, E. Mandelkow*

*Corresponding author for this work
36 Citations (Scopus)


The binding stoichiometry of kinesin to microtubules was determined using several biochemical and biophysical approaches (chemical crosslinking, binding assays, scanning transmission electron microscopy (STEM), image reconstruction, and X-ray scattering). The results show that each tubulin dimer associates with one kinesin head, irrespective of whether kinesin occurs in a monomeric or dimeric form in solution. Moreover, these heads appear to align along the protofilament axis generating a 16 nm periodicity of successive kinesin dimers. This is consistent with a 'tightrope' model of movement where the first head of the dimer provides a guiding signal for the following one.

Original languageEnglish
JournalJournal of Molecular Biology
Issue number5
Pages (from-to)795-809
Number of pages15
Publication statusPublished - 06.02.1998


Dive into the research topics of 'Interaction of monomeric and dimeric kinesin with microtubules'. Together they form a unique fingerprint.

Cite this