Laboratory of Cell Motility


Takahide KON
Assistant Professor

Functional Biomolecular Biology


Department of Biological Sciences, Graduate School of Science



Research Theme

In the cells that make up our bodies, a wide variety of macromolecules including proteins move quickly at the velocity of several meters per second using thermal energy. However, that is not useful for the long-distance transportation to the specific direction in the cells because the direction of the thermal motion is random. For example, in an elongated neuron with the length of 1 m, it will take more than 100 years to transport an average-sized protein from the cell body to the nerve terminal by the thermal motion. Eukaryotic cells manage this problem by establishing intracellular transport systems that powers a wide variety of fundamental biological processes including ciliary beating, cell division, cell migration and active transport of numerous cargoes. The partial loss of the function has been implicated in neurodegenerative disease, infertility and developmental abnormality. Our laboratory aims to elucidate the molecular mechanism underlying the intracellular transport system by means of atomic-level structural analysis and single-molecule functional analysis. Recently, we have focused on a huge motor protein complex, dynein, which is the heart of the transport system toward the center of the cells, and determined its atomic structures. We have also started a project to achieve a comprehensive understanding of mRNA transport systems in neurons.


0Atomic structure of “Dynein”, the heart of the transport system.


Imai, H. et al. Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules. Nature Commun. 2015, 6 , 8179 -

Roberts, A.J. et al. Functions and mechanics of dynein motor proteins Nature Rev. Mol. Cell Biol. 2013, 14 , 713 - 726

Kon, T. et al. The 2.8 Å crystal structure of the dynein motor domain. Nature 2012, 484 , 345 - 350

Kon, T. et al. X-ray structure of a functional full-length dynein motor domain. Nature Struct Mol Biol. 2011 18 , 638 - 642

Kon, T. et al. Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding. Nature Struct. Mol. Biol. 2009, 16 , 325 - 333

Roberts, A.J. et al. AAA+ ring and linker swing mechanism in the dynein motor. Cell. 2009, 136 , 485 - 495

Kon, T. et al. ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein Nature Struct. Mol. Biol. 2005, 12 , 513 - 519


Department of Biological Sciences
Graduate School of Science
Osaka University
1-1 Machikaneyama-cho
Toyonaka, Osaka 560-0043
Tel: +81-6-6850-5435