Yong Tang and Utpal Das contributed equally to this work.
The slow axonal transport of alpha-synuclein—mechanistic commonalities amongst diverse cytosolic cargoes†
Article first published online: 2 MAR 2012
Copyright © 2012 Wiley Periodicals, Inc.
Special Issue: Emerging Concepts in Neuronal Cytoskeleton
Volume 69, Issue 7, pages 506–513, July 2012
How to Cite
Tang, Y., Das, U., Scott, D. A. and Roy, S. (2012), The slow axonal transport of alpha-synuclein—mechanistic commonalities amongst diverse cytosolic cargoes. Cytoskeleton, 69: 506–513. doi: 10.1002/cm.21019
Monitoring Editor: Peter Bass
- Issue published online: 6 JUL 2012
- Article first published online: 2 MAR 2012
- Accepted manuscript online: 16 FEB 2012 03:14PM EST
- Manuscript Accepted: 9 FEB 2012
- Manuscript Revised: 7 FEB 2012
- Manuscript Received: 21 DEC 2011
- March Of Dimes (Basil O'Connor award)
- NIH. Grant Number: R01NS075233
Vol. 70, Issue 4, 240, Article first published online: 26 MAR 2013
- cytosolic synaptic proteins;
- slow axonal transport;
- transport packets;
- cargo complexes;
- slow component-b, SCb
Slow axonal transport conveys perikaryally-synthesized cytosolic proteins in a rate-class called Slow Component-b (SCb). One such protein—α-synuclein—is largely conveyed in SCb, and is also a key player in a group of neurodegenerative diseases called synucleinopathies. Axonal transport defects of α-synuclein have been hypothesized to play a role in synucleinopathies, but mechanisms moving α-synuclein in slow axonal transport are unclear. Here we use a recently developed model-system in our laboratory to visualize the slow transport of α-synuclein, comparing it to another SCb protein synapsin. Despite differences inbiological properties and overallsolubility in axons, the anterograde transport of both SCb proteins was strikingly similar, suggesting commonalities in slow axonal transport mechanisms of seemingly diverse cytosolic cargoes. The data support a model where SCb proteins dynamically organize into ‘transport-competent’ complexes that are conveyed via transient associations with other persistently-moving cargoes (“mobile-units”). The identity of the latter is yet unknown. Visualizing normal α-synuclein transport may also open the door to studies of α-synuclein transport in pathologic states. © 2012 Wiley Periodicals, Inc.