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Published 21 November 2005. doi:10.1083/jcb.200502043
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 4, 615-625
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Article

 Coordinated transport of phosphorylated amyloid-ß precursor protein and c-Jun NH2-terminal kinase–interacting protein-1

Zoia Muresan and Virgil Muresan

Department of Physiology and Biophysics, Case School of Medicine, Case Western Reserve University, Cleveland, OH 44106

Correspondence to Zoia Muresan: zoia.muresan{at}case.edu; or Virgil Muresan: virgil.muresan{at}case.edu

The transmembrane protein amyloid-ß precursor protein (APP) and the vesicle-associated protein c-Jun NH2-terminal kinase–interacting protein-1 (JIP-1) are transported into axons by kinesin-1. Both proteins may bind to kinesin-1 directly and can be transported separately. Because JIP-1 and APP can interact, kinesin-1 may recruit them as a complex, enabling their cotransport. In this study, we tested whether APP and JIP-1 are transported together or separately on different vesicles. We found that, within the cellular context, JIP-1 preferentially interacts with Thr668-phosphorylated APP (pAPP), compared with nonphosphorylated APP. In neurons, JIP-1 colocalizes with vesicles containing pAPP and is excluded from those containing nonphosphorylated APP. The accumulation of JIP-1 and pAPP in neurites requires kinesin-1, and the expression of a phosphomimetic APP mutant increases JIP-1 transport. Down-regulation of JIP-1 by small interfering RNA specifically impairs transport of pAPP, with no effect on the trafficking of nonphosphorylated APP. These results indicate that the phosphorylation of APP regulates the formation of a pAPP–JIP-1 complex that accumulates in neurites independent of nonphosphorylated APP.

Abbreviations used in this paper: APP, amyloid-ß precursor protein; JIP-1, JNK-interacting protein-1; JNK, c-Jun NH2-terminal kinase; KHC, kinesin heavy chain; KLC, kinesin light chain; pAPP, Thr668-phosphorylated APP; PP5, protein phosphatase 5; siRNA, small interfering RNA; TPR, tetratricopeptide repeat.


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