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Vol. 10, Issue 7, 2191-2197, July 1999
Department of Biochemistry, Stanford University School of Medicine,
Stanford, California 94305-5307
Late endosomes and the Golgi complex maintain their cellular
localizations by virtue of interactions with the microtubule-based cytoskeleton. We study the transport of mannose 6-phosphate receptors from late endosomes to the trans-Golgi network in vitro.
We show here that this process is facilitated by microtubules and the microtubule-based motor cytoplasmic dynein; transport is inhibited by
excess recombinant dynamitin or purified microtubule-associated proteins. Mapmodulin, a protein that interacts with the
microtubule-associated proteins MAP2, MAP4, and tau, stimulates the
microtubule- and dynein-dependent localization of Golgi complexes in
semi-intact Chinese hamster ovary cells. The present study shows
that mapmodulin also stimulates the initial rate with which mannose
6-phosphate receptors are transported from late endosomes to the
trans-Golgi network in vitro. These findings represent
the first indication that mapmodulin can stimulate a vesicle transport
process, and they support a model in which the microtubule-based
cytoskeleton enhances the efficiency of vesicle transport between
membrane-bound compartments in mammalian cells.
Present address: Department of Food Engineering and
Biotechnology, The Technion, 32000 Haifa, Israel.
Corresponding author. E-mail address:
pfeffer{at}cmgm.stanford.edu.
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