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Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I.

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-I), by binding directly to the TPR domain of the kinesin light chain (KLC) subunit. The estimated apparent Kd 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-I and that KLC is important for kinesin-I-driven transport of APP into axons.

Pubmed ID: 11144355


  • Kamal A
  • Stokin GB
  • Yang Z
  • Xia CH
  • Goldstein LS



Publication Data

November 20, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM35252

Mesh Terms

  • Alzheimer Disease
  • Amyloid beta-Protein Precursor
  • Animals
  • Axonal Transport
  • Binding, Competitive
  • Blotting, Western
  • Brain Chemistry
  • Centrifugation, Density Gradient
  • Epitopes
  • Gene Targeting
  • Kinesin
  • Mice
  • Mice, Mutant Strains
  • Microtubule-Associated Proteins
  • Microtubules
  • Precipitin Tests
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Sciatic Nerve