Affiliation:
1. Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892
Abstract
We show that the chaperone AAGAB binds the adaptor protein 4 (AP-4) ε and σ4 subunits, stabilizing them for assembly of the AP-4 complex. In the absence of AAGAB, AP-4 subunits are degraded by the proteasome, levels of the AP-4 complex are reduced, and the AP-4-cargo protein ATG9A accumulates at the TGN, all phenotypes resembling AP-4 deficiency.
Publisher
American Society for Cell Biology (ASCB)
Subject
Cell Biology,Molecular Biology
Cited by
3 articles.
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