
TGN46 plays a crucial role in sorting secretory cargo proteins into transport carriers at the trans-Golgi network, as demonstrated by its necessity for cargo loading into CARTS. The lumenal domain of TGN46 is identified as essential and sufficient for this sorting function.


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Secretory proteins are sorted at the trans-Golgi network (TGN) for export into specific transport carriers. However, the molecular players involved in this fundamental process remain largely elusive. Here, we identified the human transmembrane protein TGN46 as a receptor for the export of secretory cargo protein PAUF in CARTS – a class of protein kinase D-dependent TGN-to-plasma membrane carriers. We show that TGN46 is necessary for cargo sorting and loading into nascent carriers at the TGN. By combining quantitative fluorescence microscopy and mutagenesis approaches, we further discovered that the lumenal domain of TGN46 encodes for its cargo sorting function. In summary, our results define a cellular function of TGN46 in sorting secretory proteins for export from the TGN.

### Competing Interest Statement

The authors have declared no competing interest.

Sorting of secretory proteins at the trans-Golgi network by human TGN46

sorting-of-secretory-proteins-at-the-trans-golgi-network-by-tgn46-revealed


Sorting of Secretory Proteins at the Trans-Golgi Network by TGN46 Revealed
