Extended Data Figure 8 ∣. Nucleotide and force-induced release of Dyn and Dyn_RK+7hep monomers from MTs.

a, The normalized intensity of 100 nM GFP-tagged Dyn and Dyn_RK+7hep monomers on sea urchin axonemes under given nucleotide conditions. Similar to Dyn, Dyn_RK+7hep released from MTs in the ADP-Pi state, mimicked by ATP and vanadate (Vi, n = 40 axonemes from three independent measurements, mean ± s.d.). p-values are calculated from a two-sided t-test. b, A model of the dynein-MT interaction shows two distinct binding modes in the apo state, with k₁ and k₂ representing force-induced release rates from the weak and strong states, respectively. The slow rate (k₂) represents strong binding of the motor to its tubulin binding site, whereas the fast rate (k₁) represents transient or nonspecific interactions of the motor with the MT. c, Cumulative probability distributions (solid circles) of the MT-bound time of Dyn monomers at given force ranges. The release rates (k₁ and k₂) were calculated by a two-exponential-decay fit (solid curves). d, Calculated k₁ values from the exponential fit (±95% confidence intervals) to the Dyn_RK+7hep dwell time has similar force-dependence to Dyn. Each bin contains 120 dwells from two independent measurements.