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APache Is an AP2-Interacting Protein Involved in Synaptic Vesicle Trafficking and Neuronal Development.

Authors: Piccini, Alessandra  Castroflorio, Enrico  Valente, Pierluigi  Guarnieri, Fabrizia C  Aprile, Davide  Michetti, Caterina  Bramini, Mattia  Giansante, Giorgia  Pinto, Bruno  Savardi, Annalisa  Cesca, Fabrizia  Bachi, Angela  Cattaneo, Angela  Wren, Jonathan D  Fassio, Anna  Valtorta, Flavia  Benfenati, Fabio  Gioved√¨, Silvia 
Citation: Piccini A, etal., Cell Rep. 2017 Dec 19;21(12):3596-3611. doi: 10.1016/j.celrep.2017.11.073.
Pubmed: (View Article at PubMed) PMID:29262337
DOI: Full-text: DOI:10.1016/j.celrep.2017.11.073

Synaptic transmission is critically dependent on synaptic vesicle (SV) recycling. Although the precise mechanisms of SV retrieval are still debated, it is widely accepted that a fundamental role is played by clathrin-mediated endocytosis, a form of endocytosis that capitalizes on the clathrin/adaptor protein complex 2 (AP2) coat and several accessory factors. Here, we show that the previously uncharacterized protein KIAA1107, predicted by bioinformatics analysis to be involved in the SV cycle, is an AP2-interacting clathrin-endocytosis protein (APache). We found that APache is highly enriched in the CNS and is associated with clathrin-coated vesicles via interaction with AP2. APache-silenced neurons exhibit a severe impairment of maturation at early developmental stages, reduced SV density, enlarged endosome-like structures, and defects in synaptic transmission, consistent with an impaired clathrin/AP2-mediated SV recycling. Our data implicate APache as an actor in the complex regulation of SV trafficking, neuronal development, and synaptic plasticity.

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CRRD Object Information
CRRD ID: 13601995
Created: 2018-05-26
Species: All species
Last Modified: 2018-05-26
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.