Diagram of the intact dynein being present in the cells, and the genetically modified dynein used in this study. Dynein is made of a single long polypeptide, consisting of three parts; (1) ~13-nm diameter ring, which hydrolyzes ATP, the chemical energy in the cells, (2) the extension structure (10 nm long with 2 nm diameter) from the ring, which is called the “stalk” (the tip of the stalk contains microtubule-binding site), and (3) the tail structure, which connects two rings. The (minimum) motor domain consists of the ring and the stalk without the tail.
September 15, 2015
Mechanism for operating molecular motors facilitating transport of intracellular cargos clarified
A research group of Japanese universities, RIKEN and Leeds University in the UK succeeded in directly observing dynein, a motor protein facilitating transport of intracellular cargos, by using a low temperature electron microscope.
If the visualization of mutant dynein, which is related to various diseases, is achieved, it is anticipated that it will lead to the clarification of causes of neural diseases and growth disorder and the development of their treatments. It is also expected that it will lead to the elucidation of causes of cancer and applications to cancer treatment.
This research was featured in the electronic version of Nature Communications (UK) on Monday, September 14, 2015, Japan time.
