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The Journal of Neuroscience, March 21, 2007, 27(12):3131-3138; doi:10.1523/JNEUROSCI.4999-06.2007

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Cellular/Molecular
Rapid and Intermittent Cotransport of Slow Component-b Proteins

Subhojit Roy,^1,2 Matthew J. Winton,¹ Mark M. Black,⁴ John Q. Trojanowski,^1,2,3 and Virginia M.-Y. Lee^1,2,3

¹Center for Neurodegenerative Disease Research, ²Department of Pathology and Laboratory Medicine, and ³Institute on Aging, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, and ⁴Department of Anatomy and Cell Biology, Temple University Hospital, Philadelphia, Pennsylvania 19130

Correspondence should be addressed to Dr. Virginia M.-Y. Lee, Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Maloney Building, 3rd Floor, 3600 Spruce Street, Philadelphia, PA 19104. Email: vmylee{at}mail.med.upenn.edu

After synthesis in neuronal perikarya, proteins destined for synapses and other distant axonal sites are transported in three major groups that differ in average velocity and protein composition: fast component (FC), slow component-a (SCa), and slow component-b (SCb). The FC transports mainly vesicular cargoes at average rates of 200–400 mm/d. SCa transports microtubules and neurofilaments at average rates of 0.2–1 mm/d, whereas SCb translocates 200 diverse proteins critical for axonal growth, regeneration, and synaptic function at average rates of 2–8 mm/d. Several neurodegenerative diseases are characterized by abnormalities in one or more SCb proteins, but little is known about mechanisms underlying SCb compared with FC and SCa. Here, we use live-cell imaging to visualize and quantify the axonal transport of three SCb proteins, -synuclein, synapsin-I, and glyceraldehyde-3-phosphate dehydrogenase in cultured hippocampal neurons, and directly compare their transport to synaptophysin, a prototypical FC protein. All three SCb proteins move rapidly but infrequently with pauses during transit, unlike synaptophysin, which moves much more frequently and persistently. By simultaneously visualizing the transport of proteins at high temporal and spatial resolution, we show that the dynamics of -synuclein transport are distinct from those of synaptophysin but similar to other SCb proteins. Our observations of the cotransport of multiple SCb proteins in single axons suggest that they move as multiprotein complexes. These studies offer novel mechanistic insights into SCb and provide tools for further investigating its role in disease processes.

Key words: axonal transport; slow transport; slow component-b; -synuclein; synaptophysin; protein complexes

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Received Nov. 17, 2006; revised Jan. 9, 2007; accepted Feb. 6, 2007.

Correspondence should be addressed to Dr. Virginia M.-Y. Lee, Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Maloney Building, 3rd Floor, 3600 Spruce Street, Philadelphia, PA 19104. Email: vmylee{at}mail.med.upenn.edu

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