Dynein and kinesin share an overlapping microtubule-binding site

Dyneins and kinesins move in opposite directions on microtubules. The question of how the same‐track microtubules are able to support movement in two directions remains unanswered due to the absence of details on dynein–microtubule interactions. To address this issue, we studied dynein–microtubule i...

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Bibliographic Details
Published in:The EMBO journal 2004-07, Vol.23 (13), p.2459-2467
Main Authors: Mizuno, Naoko, Toba, Shiori, Edamatsu, Masaki, Watai-Nishii, Junko, Hirokawa, Nobutaka, Toyoshima, Yoko Y, Kikkawa, Masahide
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Binding, Competitive
Cattle
Corn
Cross-Linking Reagents - pharmacology
cryo-electron microscopy
Cryoelectron Microscopy
Dimerization
Drosophila
Drosophila Proteins - chemistry
Drosophila Proteins - drug effects
Drosophila Proteins - genetics
Drosophila Proteins - metabolism
Drosophila Proteins - ultrastructure
dynein
Dyneins - chemistry
Dyneins - drug effects
Dyneins - genetics
Dyneins - metabolism
Dyneins - ultrastructure
Electrophoresis, Polyacrylamide Gel
Imaging, Three-Dimensional
kinesin
Kinesin - metabolism
Kinesin - ultrastructure
Kinetics
Microtubules - chemistry
Microtubules - metabolism
Models, Biological
Models, Molecular
Models, Structural
Protein Conformation
protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Swine
tubulin
Tubulin - chemistry
Tubulin - metabolism
Tubulin - ultrastructure
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Summary:Dyneins and kinesins move in opposite directions on microtubules. The question of how the same‐track microtubules are able to support movement in two directions remains unanswered due to the absence of details on dynein–microtubule interactions. To address this issue, we studied dynein–microtubule interactions using the tip of the microtubule‐binding stalk, the dynein stalk head (DSH), which directly interacts with microtubules upon receiving conformational change from the ATPase domain. Biochemical and cryo‐electron microscopic studies revealed that DSH bound to tubulin dimers with a periodicity of 80 Å, corresponding to the step size of dyneins. The DSH molecule was observed as a globular corn grain‐like shape that bound the same region as kinesin. Biochemical crosslinking experiments and image analyses of the DSH–kinesin head–microtubule complex revealed competition between DSH and the kinesin head for microtubule binding. Our results demonstrate that dynein and kinesin share an overlapping microtubule‐binding site, and imply that binding at this site has an essential role for these motor proteins.
ISSN:0261-4189
1460-2075
DOI:10.1038/sj.emboj.7600240