Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 28, Issue 1, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/s41594-020-00530-0
Keywords
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Funding
- BCMP-Merck postdoctoral fellowship
- NIH [R01-GM081871, R00-AG050749]
- MIT J-Clinic for Machine Learning and Health
- NIGMS grant [R35-GM131909]
- E. Matilda Ziegler Foundation for the Blind
- Smith Family Foundation
- Pew Charitable Trusts
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Cryo-EM structures of radial spokes and nexin-dynein regulatory complex (N-DRC) attached to doublet microtubules isolated from Chlamydomonas reinhardtii provide a model for mechanoregulation of motile cilia.
In motile cilia, a mechanoregulatory network is responsible for converting the action of thousands of dynein motors bound to doublet microtubules into a single propulsive waveform. Here, we use two complementary cryo-EM strategies to determine structures of the major mechanoregulators that bind ciliary doublet microtubules in Chlamydomonas reinhardtii. We determine structures of isolated radial spoke RS1 and the microtubule-bound RS1, RS2 and the nexin-dynein regulatory complex (N-DRC). From these structures, we identify and build atomic models for 30 proteins, including 23 radial-spoke subunits. We reveal how mechanoregulatory complexes dock to doublet microtubules with regular 96-nm periodicity and communicate with one another. Additionally, we observe a direct and dynamically coupled association between RS2 and the dynein motor inner dynein arm subform c (IDAc), providing a molecular basis for the control of motor activity by mechanical signals. These structures advance our understanding of the role of mechanoregulation in defining the ciliary waveform. Cryo-EM structures of radial spokes and nexin-dynein regulatory complex (N-DRC) attached to doublet microtubules isolated from Chlamydomonas reinhardtii provide a model for mechanoregulation of motile cilia.
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