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Dynein structure and function.
K A Johnson1, S P Marchese-Ragona, D B Clutter
1Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
Journal of Cell Science. Supplement
|January 1, 1986
Summary
Dynein motor proteins possess three heads, each with an ATPase site, enabling them to interact with microtubules. This interaction generates force for cellular movement via an ATP-dependent sliding mechanism.
Area of Science:
- Cell Biology
- Molecular Motors
- Biochemistry
Background:
- Dynein, a crucial motor protein, is essential for various cellular functions.
- The structure of Tetrahymena 22S dynein provided an initial model for dynein organization.
Purpose of the Study:
- To elucidate the structural and functional relationship of dynein's multiple heads.
- To interpret in situ dynein images based on current biochemical data.
Main Methods:
- Isolation of dynein from various biological sources.
- Biochemical analysis to identify ATPase sites.
- Microscopic imaging of dynein in its cellular context (in situ).
Main Results:
- Dynein structure consistently features three globular heads linked to a base.
- Each head contains a single ATPase site.
- All three heads engage with microtubules in an ATP-dependent manner.
Conclusions:
- A model for dynein crossbridge action is proposed.
- Dynein anchors to A-tubules via its base.
- Heads interact with B-tubules to generate force for microtubule sliding, driven by ATP.