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. Author manuscript; available in PMC: 2012 Jan 25.
Published in final edited form as: Curr Biol. 2011 Jan 13;21(2):154–160. doi: 10.1016/j.cub.2010.12.038

Figure 1. A microtubule binding site near the kinesin-5 C-terminus allows one dimensional diffusion of microtubules.

Figure 1

(A) Domain structures of kinesin-5 GFP-fusion constructs used in this study. (B) Schematic of the single molecule microtubule interaction assay. Rhodamine-labeled microtubules were immobilized on a glass surface and the interaction of Kin5-Δmotor-GFP was observed by single molecule TIRF microscopy. (C) Images showing Kin5-Δmotor-GFP binding to surface immobilized microtubules (top: microtubule; center: single frame; bottom: time average over 300 frames). Bar: 4µm. (D) kymograph shows Kin5-Δmotor-GFP interactions with microtubules. Bar: 4µm. (E) Schematic of the surface binding assay. (F–G) Kymographs show the movement of microtubules attached to a glass surface by Kin5-Δmotor-GFP in low salt buffer (F) and high salt buffer (G) Bars: 2 µm, 60 sec. (H) MSD calculated from motion of surface-adhered microtubules in high salt buffer (●) and low salt buffer (○). Fits represent MSD = 2Dt, error bars = sem. See also Figure S1 and Movies S1–S2.