Abstract：
:GABAB receptors (GBRs) are key regulators of synaptic release but little is known about trafficking mechanisms that control their presynaptic abundance. We now show that sequence-related epitopes in APP, AJAP-1 and PIANP bind with nanomolar affinities to the N-terminal sushi-domain of presynaptic GBRs. Of the three interacting proteins, selectively the genetic loss of APP impaired GBR-mediated presynaptic inhibition and axonal GBR expression. Proteomic and functional analyses revealed that APP associates with JIP and calsyntenin proteins that link the APP/GBR complex in cargo vesicles to the axonal trafficking motor. Complex formation with GBRs stabilizes APP at the cell surface and reduces proteolysis of APP to Aβ, a component of senile plaques in Alzheimer's disease patients. Thus, APP/GBR complex formation links presynaptic GBR trafficking to Aβ formation. Our findings support that dysfunctional axonal trafficking and reduced GBR expression in Alzheimer's disease increases Aβ formation.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Dinamarca MC,Raveh A,Schneider A,Fritzius T,Früh S,Rem PD,Stawarski M,Lalanne T,Turecek R,Choo M,Besseyrias V,Bildl W,Bentrop D,Staufenbiel M,Gassmann M,Fakler B,Schwenk J,Bettler Bdoi
10.1038/s41467-019-09164-3subject
Has Abstractpub_date
2019-03-22 00:00:00pages
1331issue
1issn
2041-1723pii
10.1038/s41467-019-09164-3journal_volume
10pub_type
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