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The Journal of Neuroscience, March 2, 2005, 25(9):2386-2395; doi:10.1523/JNEUROSCI.3089-04.2005

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Neurobiology of Disease
Axonal Transport, Amyloid Precursor Protein, Kinesin-1, and the Processing Apparatus: Revisited

Orly Lazarov,1 * Gerardo A. Morfini,2 * Edward B. Lee,3 Mohamed H. Farah,4 Anita Szodorai,5 Scott R. DeBoer,2 Vassilis E. Koliatsos,4 Stefan Kins,5 Virginia M.-Y. Lee,3 Philip C. Wong,4 Donald L. Price,4 Scott T. Brady,2 and Sangram S. Sisodia1

1Department of Neurobiology, Pharmacology, and Physiology, The University of Chicago, Chicago, Illinois 60637, 2Department of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois 60612, 3Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, 4Department of Pathology, Division of Neuropathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and 5Center of Molecular Biology Heidelberg, University of Heidelberg, D-69120 Heidelberg, Germany

The sequential enzymatic actions of {beta}-APP cleaving enzyme 1 (BACE1), presenilins (PS), and other proteins of the {gamma}-secretase complex liberate {beta}-amyloid (A{beta}) peptides from larger integral membrane proteins, termed {beta}-amyloid precursor proteins (APPs). Relatively little is known about the normal function(s) of APP or the neuronal compartment(s) in which APP undergoes proteolytic processing. Recent studies have been interpreted as consistent with the idea that APP serves as a kinesin-1 cargo receptor and that PS and BACE1 are associated with the APP-resident membranous cargos that undergo rapid axonal transport. In this report, derived from a collaboration among several independent laboratories, we examined the potential associations of APP and kinesin-1 using glutathione S-transferase pull-down and coimmunoprecipitation assays. In addition, we assessed the trafficking of membrane proteins in the sciatic nerves of transgenic mice with heterozygous or homozygous deletions of APP. In contrast to previous reports, we were unable to find evidence for direct interactions between APP and kinesin-1. Furthermore, the transport of kinesin-1 and tyrosine kinase receptors, previously reported to require APP, was unchanged in axons of APP-deficient mice. Finally, we show that two components of the APP proteolytic machinery, i.e., PS1 and BACE1, are not cotransported with APP in the sciatic nerves of mice. These findings suggest that the hypothesis that APP serves as a kinesin-1 receptor and that the proteolytic processing machinery responsible for generating A{beta} is transported in the same vesicular compartment in axons of peripheral nerves requires revision.

Key words: APP; presenilin; kinesin-1; axonal transport; Alzheimer's disease; proteolysis

Received July 29, 2004; revised January 20, 2005; accepted January 20, 2005.




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