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Amyloid precursor protein is trafficked and secreted via synaptic vesicles.


ABSTRACT: A large body of evidence has implicated amyloid precursor protein (APP) and its proteolytic derivatives as key players in the physiological context of neuronal synaptogenesis and synapse maintenance, as well as in the pathology of Alzheimer's Disease (AD). Although APP processing and release are known to occur in response to neuronal stimulation, the exact mechanism by which APP reaches the neuronal surface is unclear. We now demonstrate that a small but relevant number of synaptic vesicles contain APP, which can be released during neuronal activity, and most likely represent the major exocytic pathway of APP. This novel finding leads us to propose a revised model of presynaptic APP trafficking that reconciles existing knowledge on APP with our present understanding of vesicular release and recycling.

SUBMITTER: Groemer TW 

PROVIDER: S-EPMC3083403 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Amyloid precursor protein is trafficked and secreted via synaptic vesicles.

Groemer Teja W TW   Thiel Cora S CS   Holt Matthew M   Riedel Dietmar D   Hua Yunfeng Y   Hüve Jana J   Wilhelm Benjamin G BG   Klingauf Jürgen J  

PloS one 20110427 4


A large body of evidence has implicated amyloid precursor protein (APP) and its proteolytic derivatives as key players in the physiological context of neuronal synaptogenesis and synapse maintenance, as well as in the pathology of Alzheimer's Disease (AD). Although APP processing and release are known to occur in response to neuronal stimulation, the exact mechanism by which APP reaches the neuronal surface is unclear. We now demonstrate that a small but relevant number of synaptic vesicles cont  ...[more]

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