Abstract
The means by which the neuron regulates axonal transport of cargo remains an open field for study. Recent experiments examining Huntington's disease (HD) have revealed a molecular basis underlying fast axonal transport deficits characteristic of HD. This mechanism involves activation of JNK3 and JNK3-mediated phosphorylation of the kinesin-1 heavy chain (KHC) at serine 176. We have generated a phosphomimetic KHC construct (S176D) to characterize the effects phosphorylation has on kinesin's ability to translocate along microtubules. Using total internal reflection florescence (TIRF) microscopy, we have measured a dramatic reduction in the processive run length of S176D, as compared to the unphosphorylatable variant S176A. While this observation reveals a mechanism by which neurons control anterograde trafficking, it also suggests a mechanism for tuning the bidirectional transport of vesicles by kinesin and dynein.
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