Journal
NEURON
Volume 28, Issue 2, Pages 449-459Publisher
CELL PRESS
DOI: 10.1016/S0896-6273(00)00124-0
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Funding
- NIGMS NIH HHS [GM35252] Funding Source: Medline
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We analyzed the mechanism of axonal transport of the amyloid precursor protein (APP), which plays a major role in the development of Alzheimer's disease. Coimmunoprecipitation, sucrose gradient, and direct in vitro binding demonstrated that APP forms a complex with the microtubule motor, conventional kinesin (kinesin-1), by binding directly to the TPR domain of the kinesin light chain (KLC) subunit. The estimated apparent K-d for binding is 15-20 nM, with a binding stoichiometry of two APP per KLC. In addition, association of APP with microtubules and axonal transport of APP is greatly decreased in a gene-targeted mouse mutant of the neuronally enriched KLC1 gene. We propose that one of the normal functions of APP may be as a membrane cargo receptor for kinesin-1 and that KLC is important for kinesin-1-driven transport of APP into axons.
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