Regulatory roles of the four ATPase sites in the dynein motor domain

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K18514
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics
• Research Institution: The University of Tokyo
• Principal Investigator: Shima Tomohiro 東京大学, 大学院理学系研究科(理学部), 助教 (60631786)
• Research Collaborator: UEMURA Sotaro
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: 協同性

Outline of Final Research Achievements

Cytoplasmic dynein moves along microtubule using energy of ATP. This movement enrolls in a wide variety of cellular processes including mitosis, organelle positioning, and intra-cellular trafficking. One of the unique features of dynein is that the dynein motor domain contains four ATP binding sites. Although regulation between these four ATP binding sites seems to be critical for the dynein motility, it remains unanswered how dynein uses these four ATP binding sites. Here, we tried and succeeded in visualizing the binding and release of ATP molecules on single moledcules of dynein.

Free Research Field

生物物理