Nucleotide-dependent behavior of single molecules of cytoplasmic dynein on microtubules in vitro

作者：Miura Michi; Matsubara Aiko; Kobayashi Takuya; Edamatsu Masaki; Toyoshima Yoko Y^*

来源：FEBS LETTERS, 2010, 584(11): 2351-2355.

DOI：10.1016/j.febslet.2010.04.016

• Cytoplasmic dynein
• Dynactin
• p150
• Single molecule
• Microtubule

We visualized the nucleotide-dependent behavior of single molecules of mammalian native cytoplasmic dynein using fragments of dynactin p150 with or without its N-terminal microtubule binding domain. The results indicate that the binding affinity of dynein for microtubules is high in AMPPNP, middle in ADP or no nucleotide, and low in ADP.Pi conditions. It is also demonstrated that the microtubule binding domain of dynactin p150 maintains the association of dynein with microtubules without altering the motile property of dynein in the weak binding state. In addition, we observed bidirectional movement of dynein in the presence of ATP as well as in ADP/Vi condition, suggesting that the bidirectional movement is driven by diffusion rather than active transport.

• 出版日期2010-6-3