@article{22306,
  abstract     = {The AP3 complex mediates cargo sorting and carrier assembly for the trafficking of transmembrane proteins from endosomes to lysosomes. AP3 is generally believed to localize to clathrin-free, ARF1-positive, elongated carriers in cells, but the architecture of AP3-based coats was unknown. Using in vitro reconstitution and cryo–electron tomography, we demonstrate that AP3:ARF1 spontaneously remodels membranes containing cargo and the phosphoinositide PI(3,5)P
                    <jats:sub>2</jats:sub>
                    into tubular structures coated in spiraling rows of AP3 arches and ARF1 dimers. Targeted point mutations disrupting critical AP3:ARF1 and AP3:AP3 lattice interfaces disrupt AP3 recruitment, carrier formation, and lysosomal cargo trafficking in cells. We propose that AP3 generates tubular carriers on endosomes by organizing ARF1 dimers into elongated membrane-deforming arrays while simultaneously selecting cargo. By demonstrating that AP3:ARF1 can generate carriers without using a clathrin lattice, we explain the clathrin independence of AP3-mediated trafficking.},
  author       = {Kaufman, Jonathan G.G. and Tagiltsev, Grigory and Stalder, Danièle S. and Taylor, Rebecca J. and Sava, Ioana and Guo, Hui and Ciazynska, Katarzyna A. and Zaccai, Nathan R. and Gray, Sally R. and Vallis, Yvonne and Höning, Stefan and Kelly, Bernard T. and Gershlick, David C. and Briggs, John A.G. and Owen, David J.},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {20},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Architecture of clathrin-independent AP3:ARF1-coated carriers}},
  doi          = {10.1126/sciadv.aed1529},
  volume       = {12},
  year         = {2026},
}