Proteomics

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


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 co-expressing 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 start to sequester cargo by 30 minutes 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.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Robin Antrobus  

LAB HEAD: Margaret S. Robinson

PROVIDER: PXD050449 | Pride | 2024-04-03

REPOSITORIES: Pride

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