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

doi:10.1006/jmbi.1997.1503

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

Institute of Physics

36 Citations (Scopus)

Abstract

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 language	English
Journal	Journal of Molecular Biology
Volume	275
Issue number	5
Pages (from-to)	795-809
Number of pages	15
ISSN	0022-2836
DOIs	https://doi.org/10.1006/jmbi.1997.1503
Publication status	Published - 06.02.1998

Funding

This work was supported by grants from the Deutsche Forschungsgemeinschaft (to E.M.M.), the Swiss National Science Foundation (grant 31-39691.93), the Canton Basel-Stadt, and the M.E. Müller Foundation of Switzerland.

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title = "Interaction of monomeric and dimeric kinesin with microtubules",

abstract = "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.",

author = "M. Thorm{\"a}hlen and A. Marx and M{\"u}ller, \{S. A.\} and Song, \{Y. H.\} and Mandelkow, \{E. M.\} and U. Aebi and E. Mandelkow",

note = "Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft (to E.M.M.), the Swiss National Science Foundation (grant 31-39691.93), the Canton Basel-Stadt, and the M.E. M{\"u}ller Foundation of Switzerland. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "1998",

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AU - Thormählen, M.

AU - Marx, A.

AU - Müller, S. A.

AU - Song, Y. H.

AU - Mandelkow, E. M.

AU - Aebi, U.

AU - Mandelkow, E.

N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft (to E.M.M.), the Swiss National Science Foundation (grant 31-39691.93), the Canton Basel-Stadt, and the M.E. Müller Foundation of Switzerland. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 1998/2/6

Y1 - 1998/2/6

N2 - 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.

AB - 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.

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DO - 10.1006/jmbi.1997.1503

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JF - Journal of Molecular Biology

IS - 5

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Interaction of monomeric and dimeric kinesin with microtubules

Abstract

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