![]() They would bind the plasmid and halt transcription. Kinesin-1 motors not bound to organelles would enter the nucleus where Transcription by incorporating a nuclear localization signal and zinc finger domain in the For the smaller Kinesin-1s, we controlled Implicated in neuronal vesicle transport. To overcome this problem, we expressed only the cargo-binding tails of the kinesins Inhibited kinesins whose motor domains are bound to their cargo-binding tails. The current model argues that this soluble pool consists of Often there would be a soluble population of kinesin that likely concealed Before this method, researchers usually expressedįull-length kinesins fused to a fluorophore that provided poor and inconsistent organelle This project was only possible because of the development of a novel method to A model to explain this suggests that the C. In this model, KIF13s mediate polarized transport ofĭistinct and overlapping vesicle populations, with AP-1 performing initial recruitment of dendrites, as vesicles containing the transferrin receptor are excluded from the axon (Burack et al. However, AP-1 does not serve as the long-term kinesinĪdaptor for either vesicle population. Critically, disrupting this interaction reduces dendrite- and axon-selective I found that both motors are recruited to Golgi-derived vesicles at the transGolgi network (TGN) by binding the heterotetrameric clathrin adaptor protein (AP)Ĭomplex-1. ![]() Transporting axon-selective vesicles containing neuron-glia cell adhesion molecule Specialized for dendrite-selective transport, with KIF13B assisting but additionally Quantitative fluorescence imaging to determine that KIF13s differ in their colocalizationĪnd cotransport with dendrite-selective transferrin receptor (TfR) vesicles: KIF13A is Motors and their binding and transport of dendrite-selective vesicles is unknown. Whether there are differences between these The related kinesin-3 molecular motors, KIF13A and KIF13B, Into vesicles at the Golgi, which must recruit the correct molecular motors to confer Membrane trafficking maintains this polarity but is poorly understood.ĭendritically polarized membrane trafficking requires the sorting of dendritic proteins Unique complements of membrane proteins facilitate these functions, making neurons To facilitate this function, they possess an exotic morphology containingĬomplementary extensions: the signal-sending axon and signal-receiving dendrites. AbstractThe nervous system is comprised of neurons, which send and receive electrochemicalsignals.
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