The role of the AP-1 adaptor complex in outgoing and incoming membrane traffic.

MS Robinson, Robin Antrobus, A Sanger, AK Davies, DC Gershlick

Research output: Contribution to journalArticlepeer-review

Abstract

The AP-1 adaptor complex is found in all eukaryotes, but it has been implicated in different pathways in different organisms. To look directly at AP-1 function, we generated stably transduced HeLa cells coexpressing tagged AP-1 and various tagged membrane proteins. Live cell imaging showed that AP-1 is recruited onto tubular carriers trafficking from the Golgi apparatus to the plasma membrane, as well as onto transferrin-containing early/recycling endosomes. Analysis of single AP-1 vesicles showed that they are a heterogeneous population, which starts to sequester cargo 30 min after exit from the ER. Vesicle capture showed that AP-1 vesicles contain transmembrane proteins found at the TGN and early/recycling endosomes, as well as lysosomal hydrolases, but very little of the anterograde adaptor GGA2. Together, our results support a model in which AP-1 retrieves proteins from post-Golgi compartments back to the TGN, analogous to COPI’s role in the early secretory pathway. We propose that this is the function of AP-1 in all eukaryotes.

Original languageEnglish
Article numbere202310071
JournalThe Journal of cell biology
Volume223
Issue number7
DOIs
Publication statusPublished - 5 Apr 2024

Keywords

  • Organelles
  • Trafficking
  • Membrane Proteins/metabolism
  • trans-Golgi Network/metabolism
  • Cell Membrane/metabolism
  • Humans
  • Golgi Apparatus/genetics
  • HeLa Cells
  • Adaptor Proteins, Vesicular Transport/metabolism
  • Endosomes/genetics
  • Transcription Factor AP-1/genetics
  • Protein Transport

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