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Vol. 10, Issue 7, 2191-2197, July 1999

Mapmodulin, Cytoplasmic Dynein, and Microtubules Enhance the Transport of Mannose 6-Phosphate Receptors from Endosomes to the Trans-Golgi Network

Christian Itin,* Nirit Ulitzur,*dagger Bettina Mühlbauer, and Suzanne R. PfefferDagger

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.


*   These authors contributed equally to this work.
dagger    Present address: Department of Food Engineering and Biotechnology, The Technion, 32000 Haifa, Israel.
Dagger    Corresponding author. E-mail address: pfeffer{at}cmgm.stanford.edu.


Molecular Biology of the Cell
Vol. 10, 2191-2197, July 1999
Copyright © 1999 by The American Society for Cell Biology



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