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Vol. 10, Issue 12, 4107-4120, December 1999
§
¶#**
*Department of Cell Biology, University of Geneva, Geneva 1211, Switzerland; and The flow of material from peripheral, early endosomes to late
endosomes requires microtubules and is thought to be facilitated by the
minus end-directed motor cytoplasmic dynein and its activator dynactin.
The microtubule-binding protein CLIP-170 may also play a role by
providing an early link to endosomes. Here, we show that perturbation
of dynactin function in vivo affects endosome dynamics and trafficking.
Endosome movement, which is normally bidirectional, is completely
inhibited. Receptor-mediated uptake and recycling occur normally, but
cells are less susceptible to infection by enveloped viruses that
require delivery to late endosomes, and they show reduced accumulation
of lysosomally targeted probes. Dynactin colocalizes at microtubule
plus ends with CLIP-170 in a way that depends on CLIP-170's putative
cargo-binding domain. Overexpression studies using
p150Glued, the microtubule-binding subunit of dynactin, and
mutant and wild-type forms of CLIP-170 indicate that CLIP-170 recruits
dynactin to microtubule ends. These data suggest a new model for the
formation of motile complexes of endosomes and microtubules early in
the endocytic pathway.
Department of Biology, The Johns
Hopkins University, Baltimore, Maryland 21218
Present addresses: Department of
Experimental Medicine, Anatomy Section, University of Genova, Via De
Toni 14, 16132 Genova, Italy;
§
Medical Scientist
Training Program, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110;
Institute for
Cytobiology, Clinic of Philipps-University Marburg, Robert-Koch-Strasse
5, 35037 Marburg, Germany;
¶
Department of Anatomy and
Neuroscience, Washington University School of Medicine, 660 S. Euclid
Avenue, St. Louis, MO 63110;
#
The Institute for Genomic
Research, 9712 Medical Center Drive, Rockville, MD 20850.
**
Corresponding author. E-mail address: schroer{at}jhu.edu.
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