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Vol. 11, Issue 4, 1213-1224, April 2000
and
*European Molecular Biology Laboratory, Cell Biology Program, 69012 Heidelberg, Germany; and Neurons transport newly synthesized membrane proteins along axons
by microtubule-mediated fast axonal transport. Membrane proteins
destined for different axonal subdomains are thought to be transported
in different transport carriers. To analyze this differential transport
in living neurons, we tagged the amyloid precursor protein (APP) and
synaptophysin (p38) with green fluorescent protein (GFP) variants. The
resulting fusion proteins, APP-yellow fluorescent protein (YFP),
p38-enhanced GFP, and p38-enhanced cyan fluorescent protein, were
expressed in hippocampal neurons, and the cells were imaged by video
microscopy. APP-YFP was transported in elongated tubules that moved
extremely fast (on average 4.5 µm/s) and over long distances. In
contrast, p38-enhanced GFP-transporting structures were more vesicular
and moved four times slower (0.9 µm/s) and over shorter distances
only. Two-color video microscopy showed that the two proteins were
sorted to different carriers that moved with different characteristics
along axons of doubly transfected neurons. Antisense treatment using
oligonucleotides against the kinesin heavy chain slowed down the long,
continuous movement of APP-YFP tubules and increased frequency of
directional changes. These results demonstrate for the first time
directly the sorting and transport of two axonal membrane proteins into different carriers. Moreover, the extremely fast-moving tubules represent a previously unidentified type of axonal carrier.
Division of Neurophysiology,
National Institute for Medical Research, London NW7 1AA, United
Kingdom
Online version of this article contains video material
for Figures 4, 5, 8, and 9. Online version available at
www.molbiolcell.org.
Corresponding author. E-mail address:
dotti{at}embl-heidelberg.de.
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