Practice question

Motile cilia contain nine plus two axoneme where outer doublets composed of A and B tubules slide relative to each other when axonemal dynein arms anchored on A tubule bind and walk toward minus end of neighboring B tubule, activated in coordinated wave from base to tip. Unrestrained sliding would cause doublets to telescopically extend apart, disrupting structure. Restraint provided by nexin links now recognized as nexin-dynein regulatory complex, elastic proteinaceous bridges composed of DRC1-4 and associated proteins connecting adjacent doublets circumferentially every ninety six nanometers. They limit sliding amplitude to about sixty to seventy nanometers per beat cycle and store elastic energy that recoils to produce bending. Additional resistance from radial spokes transmitting signals from central pair regulates dynein activity. Electron tomography shows N-DRC as hook-like structures. Protease digestion generating sliding disintegration assay causes ATP-induced complete doublet separation, confirming structural role. Kinesin does not reside in axoneme, actin absent, phosphorylation tunes waveform not tethering.