Abstract
Axoplasm extruded from the squid giant axon has been used to analyse the molecular mechanisms of intracellular vesicle transport1,2. Using video-enhanced light microscopy, vesicle transport can be observed directly on individual microtubules at the edge of the axoplasm2–4. Here we report that AMP-PNP (adenyl-5′-yl imidodiphosphate), a non-hydrolysable analogue of ATP, reversibly inhibited vesicle transport. Moreover, vesicles in solution attach to the microtubules and form relatively stable complexes. AMP-PNP may produce this effect by binding to an ATP-binding site on the transport machinery, thereby stabilizing the motility complex that is normally formed by a transported vesicle, an ATPase and a microtubule. The effects of AMP-PNP on the vesicle transport system indicate that the enzymatic machinery of this system differs significantly from that of the actomyosin system or the dynein–microtubule system.
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Lasek, R., Brady, S. Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMP-PNP. Nature 316, 645–647 (1985). https://doi.org/10.1038/316645a0
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DOI: https://doi.org/10.1038/316645a0
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