NDLI: Cytoplasmic dynein is associated with slow axonal transport.

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Cytoplasmic dynein is associated with slow axonal transport.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dillman, J. F. Pfister, K. K. Dabney, L. P.
Description	Author Affiliation: Dillman JF ( Department of Cell Biology, School of Medicine, University of Virginia Health Sciences Center, Charlottesville 22908, USA.);
Abstract	Neuronal function is dependent on the transport of materials from the cell body to the synapse via anterograde axonal transport. Anterograde axonal transport consists of several components that differ in both rate and protein composition. In fast transport, membranous organelles are moved along microtubules by the motor protein kinesin. The cytoskeleton and the cytomatrix proteins move in the two components of slow transport. While the mechanisms underlying slow transport are unknown, it has been hypothesized that the movement of microtubules in slow transport is generated by sliding. To determine whether dynein, a motor protein that causes microtubule sliding in flagella, may play a role in slow axonal transport, we identified the transport rate components with which cytoplasmic dynein is associated in rat optic nerve. Nearly 80% of the anterogradely moving dynein was associated with slow transport, whereas only approximately 15% of the dynein was associated with the membranous organelles of anterograde fast axonal transport. A segmental analysis of the transport of dynein through contiguous regions of the optic nerve and tract showed that dynein is associated with the microfilaments and other proteins of slow component b. Dynein from this transport component has the capacity to bind microtubules in vitro. These results are consistent with the hypothesis that cytoplasmic dynein generates the movement of microtubules in slow axonal transport. A model is presented to illustrate how dynein attached to the slow component b complex of proteins is appropriately positioned to generate force of the correct polarity to slide microtubules down the axon.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Axonal Transport Dyneins Physiology Animals Cytoplasm Microtubules Metabolism Optic Nerve Protein Binding Rats, Sprague-Dawley Time Factors Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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