Structural insights into microtubule binding by dynein motors
- Datum
- 05.03.2020
- Zeit
- 15:00 - 16:00
- Sprecher
- Sam Lacey
- Zugehörigkeit
- MRC Laboratory of Molecular Biology, Cambridge, UK
- Sprache
- en
- Hauptthema
- Biologie
- Host
- Gaia Pigino
- Beschreibung
- Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. I will present cryo-EM structures of microtubules decorated with the MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7, as well as a new workflow to process pseudosymmetrical filaments in Relion. These structures demonstrate that dyneins control their affinity for microtubules through the movement of a single helix. The DNAH7 MTBD contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament in our structures. We observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. These findings suggest that axonemal dyneins have developed an additional way to influence their microtubule track and control the ciliary beat.
Letztmalig verändert: 06.03.2020, 00:09:26
Veranstaltungsort
Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG Galleria)Pfotenhauerstraße10801307Dresden
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- +49 351 210-0
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- +49 351 210-2000
- MPI-CBG
- Homepage
- http://www.mpi-cbg.de
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Max Planck Institute of Molecular Cell Biology and GeneticsPfotenhauerstraße10801307Dresden
- Telefon
- +49 351 210-0
- Fax
- +49 351 210-2000
- MPI-CBG
- Homepage
- http://www.mpi-cbg.de
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