Figure 9. Removal of the kinesin-1 stalk domain enhances motor landing. (A) Overview of kinesin-1 constructs used. (B) Purified K370-GFP and K560-GFP analyzed by SDS-PAGE. Protein concentrations were determined using BSA standard. (C) Kymographs of K370-GFP and K560-GFP motors moving on dynamic MTs. (D) Quantification of kinesin landing frequencies; n = 57 (K370-GFP) from three independent experiments and n = 167 (K560-GFP) from two independent experiments. ***, P < 0.001, Mann–Whitney U test. (E) Summarizing table of the characteristics and effects of MAP7 proteins on different parameters of kinesin activity observed in vitro and in cells. (F) Working model of kinesin-1 activation by MAP7 family proteins. Red lines indicate MAP–MT interactions.
Figure 9.

Removal of the kinesin-1 stalk domain enhances motor landing. (A) Overview of kinesin-1 constructs used. (B) Purified K370-GFP and K560-GFP analyzed by SDS-PAGE. Protein concentrations were determined using BSA standard. (C) Kymographs of K370-GFP and K560-GFP motors moving on dynamic MTs. (D) Quantification of kinesin landing frequencies; n = 57 (K370-GFP) from three independent experiments and n = 167 (K560-GFP) from two independent experiments. ***, P < 0.001, Mann–Whitney U test. (E) Summarizing table of the characteristics and effects of MAP7 proteins on different parameters of kinesin activity observed in vitro and in cells. (F) Working model of kinesin-1 activation by MAP7 family proteins. Red lines indicate MAP–MT interactions.

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