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FEBS Lett ; 592(16): 2716-2724, 2018 08.
Article in English | MEDLINE | ID: mdl-30055048

ABSTRACT

Amyloid ß-protein precursor (APP) is transported mainly by kinesin-1 and at a higher velocity than other kinesin-1 cargos, such as Alcadein α (Alcα); this is denoted by the enhanced fast velocity (EFV). Interaction of the APP cytoplasmic region with kinesin-1, which is essential for EFV transport, is mediated by JNK-interacting protein 1 (JIP1). To determine the roles of interactions between the APP luminal region and cargo components, we monitored transport of chimeric cargo receptors, Alcα (luminal)-APP (cytoplasmic) and APP (luminal)-Alcα (cytoplasmic). Alcα-APP is transported at the EFV, whereas APP-Alcα is transported at the same velocity as wild-type Alcα. Thus, the cytoplasmic region of APP is necessary and sufficient for the EFV of APP transport by kinesin-1.


Subject(s)
Amyloid beta-Protein Precursor/chemistry , Amyloid beta-Protein Precursor/metabolism , Cytoplasm/metabolism , Kinesins/metabolism , Neurons/metabolism , Adaptor Proteins, Signal Transducing/metabolism , Animals , Calcium-Binding Proteins , Cell Line , Humans , Mice , Protein Binding , Protein Transport
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