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. 2022 Jul 7;119(28):e2120193119. doi: 10.1073/pnas.2120193119

Fig. 2.

Fig. 2.

Single-molecule analysis of Kif4A-GFP movement in the presence of Kif4A-unlabeled. (A) Kymographs obtained from time-lapse image sequence acquired in examining microtubule interaction of Kif4A-GFP (20 pM) in presence of 0, 30, 60, 100, 200, and 400 pM Kif4A-unlabeled. Kymographs are aligned so that the plus ends of microtubules appear on the right. (B–D) Histograms of the run length (B), lifetime (C), and average velocity (D) obtained from time-lapse image sequence acquired in examining microtubule interaction of Kif4A-GFP (20 pM) in presence of 0, 30, 60, 100, 200, and 400 pM Kif4A-unlabeled. The run length and lifetime histograms were fitted to an exponential function. The average velocity histogram was fitted to a Gaussian distribution. (E) Average run length versus Kif4A concentration, obtained from the exponential fits in C: 0 pM (1,265 nm, n = 205), 30 pM (1,700 nm, n = 62), 60 pM (2,572 nm, n = 134), 100 pM (2,262 nm, n = 106), 200 pM (2,350 nm, n = 182), and 400 pM (2,946 nm, n = 78). (F) Average lifetime versus Kif4A concentration, obtained from the exponential fits in D: 0 pM (2.4 s, n = 205), 30 pM (4.3 s, n = 50, 60 pM (10 s, n = 134), 100 pM (8 s, n = 106), 200 pM (13.6 s, n = 182), and 400 pM (25 s, n = 78). (G) Average velocity versus Kif4A concentration, obtained from the Gaussian fits in E: 0 pM (562 nm/s, n = 205), 30 pM (675 nm/s, n = 43), 60 pM (336 nm/s, n = 134), 100 pM (281 nm/s, n = 106), 200 pM (291 nm/s, n = 182), and 400 pM (209 nm/s, n = 78). The error bars represent the SEM.