Complex formation of APP with GABAB receptors links axonal trafficking to amyloidogenic processing

Complex formation of APP with GABAB receptors links axonal trafficking to amyloidogenic processing

The mechanisms that control the presynaptic abundance of GABAB receptors (GBRs) remains unclear. This study shows that sequence-related epitopes in APP, AJAP-1 and PIANP bind with nanomolar affinities to the N-terminal sushi-domain of presynaptic GBRs, and that selective loss of APP impaired GBR-med...

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Autores principales: Margarita C. Dinamarca, Adi Raveh, Andy Schneider, Thorsten Fritzius, Simon Früh, Pascal D. Rem, Michal Stawarski, Txomin Lalanne, Rostislav Turecek, Myeongjeong Choo, Valérie Besseyrias, Wolfgang Bildl, Detlef Bentrop, Matthias Staufenbiel, Martin Gassmann, Bernd Fakler, Jochen Schwenk, Bernhard Bettler
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/1122aad37c3e4affaea79ae9d7612a6d
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Sumario:The mechanisms that control the presynaptic abundance of GABAB receptors (GBRs) remains unclear. This study shows that sequence-related epitopes in APP, AJAP-1 and PIANP bind with nanomolar affinities to the N-terminal sushi-domain of presynaptic GBRs, and that selective loss of APP impaired GBR-mediated presynaptic inhibition and axonal GBR expression

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