Structures of radial spokes and associated complexes important for ciliary motility.

Nat Struct Mol Biol

Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.

Published: January 2021

AI Article Synopsis

  • The study focuses on motile cilia, where a network regulates how dynein motors generate movement through doublet microtubules.
  • The researchers used cryo-electron microscopy to visualize key components, like radial spokes and the nexin-dynein regulatory complex, revealing the structures of 30 proteins crucial for ciliary function.
  • They discovered how these mechanoregulatory structures connect to microtubules and interact with each other, highlighting a specific link that controls dynein motor activity, enhancing our understanding of ciliary wave patterns.

Article Abstract

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7855293PMC
http://dx.doi.org/10.1038/s41594-020-00530-0DOI Listing

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