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Journal of Neuroscience, Vol 15, 4259-4269, Copyright © 1995 by Society for Neuroscience
Nocodazole-dependent transport, and brefeldin A--sensitive processing and sorting, of newly synthesized membrane proteins in cultured neurons
A Cid-Arregui, RG Parton, K Simons and CG Dotti
Cell Biology Program, European Molecular Biology Laboratory, Heidelberg, Germany.
The envelope glycoproteins of Semliki Forest virus (SFV), Vesicular
Stomatitis virus (VSV), and Influenza Fowl Plague virus (FPV) are
vectorially targeted in neurons to the plasma membrane of dendrites (SFV
and VSV) and axons (FPV). To gain insight into the mechanisms responsible
for such polarized delivery we have examined the effects on neurons of
nocodazole and brefeldin A (BFA), which are known to cause microtubule
depolymerization and disassembly of the Golgi apparatus, respectively.
Nocodazole treatment blocked transport of all viral glycoproteins to both
axons and dendrites. BFA treatment induced disruption of the Golgi complex,
including the trans-Golgi network (TGN), and tubulation of endosomes.
However, the delivery of the SFV and FPV glycoproteins to the cell surface
was not affected significantly by BFA, although processing and sorting were
altered, as revealed by surface biotinylation and immunofluorescence
microscopy of fixed nonpermeabilized cells. These results demonstrate the
involvement of microtubules in axonal and dendritic transport of integral
membrane glycoproteins, and the existence of a BFA-sensitive component in
the sorting but not in the transport machinery.
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