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. Author manuscript; available in PMC: 2012 Jul 2.
Published in final edited form as: Biochemistry. 2011 Nov 8;50(47):10300–10310. doi: 10.1021/bi2009147

Figure 4.

Figure 4

Hsp70 rescues anterograde FAT in isolated squid axoplasm. Vesicle motility assays in isolated squid axoplasm. Individual velocity (micrometers per second) rate measurements (arrowheads) are plotted as a function of time (minutes). Black arrowheads and lines represent anterograde FAT rates (conventional kinesin-dependent), and gray arrows and lines represent retrograde FAT rates (cytoplasmic dynein-dependent). (A) Perfusion of soluble hTau40 (2 μM) in axoplasm does not affect FAT. (B) Perfusion of tau aggregates (2 μM) results in a select inhibition of kinesin-dependent FAT as previously reported.13 (C) When Hsp70 (1.6 μM) is preincubated with the aggregated tau, no decrease in the velocity of anterograde FAT is observed [p < 0.001 (unpaired t test)], indicating that Hsp70 reverses the toxicity of tau aggregates in isolated axoplasm.