Abstract
Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length.
Highlights
Kinesin-1 is a microtubule-based motor protein that converts the chemical energy derived from ATP hydrolysis into mechanical work to translocate processively towards the plus end of a microtubule
Thereby, kinesin-1 shows a preference for axonal microtubules over dendritic microtubules [2,3] and experiments with truncated motor constructs have shown that the motor domain itself is sufficient to distinguish between the two kinds of microtubules [2]
Cells were treated with trichostatin A (TSA) – an inhibitor of the histone deacetylase (HDAC) family – which subsequently caused an increase in overall tubulin acetylation [4,6]
Summary
Kinesin-1 is a microtubule-based motor protein that converts the chemical energy derived from ATP hydrolysis into mechanical work to translocate processively towards the plus end of a microtubule. Two in vivo studies indicated that acetylation alone might not be sufficient to explain the preferential binding of kinesin-1 to axonal microtubules [10,11]. In order to analyze whether acetylation of the K40 residue alone is sufficient to modify kinesin-1 motility, we performed in vitro multi-motor gliding and single-motor stepping assays with microtubules reconstituted from acetylated and deacetylated porcine tubulin.
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