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

Autor:	Lujan P; ICFO-Institut de Ciencies Fotoniques, The Barcelona Institute of Science and Technology, Barcelona, Spain., Garcia-Cabau C; Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Spain., Wakana Y; School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan., Vera Lillo J; ICFO-Institut de Ciencies Fotoniques, The Barcelona Institute of Science and Technology, Barcelona, Spain., Rodilla-Ramírez C; ICFO-Institut de Ciencies Fotoniques, The Barcelona Institute of Science and Technology, Barcelona, Spain., Sugiura H; School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan., Malhotra V; Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, Barcelona, Spain.; Universitat Pompeu Fabra, Barcelona, Spain.; Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain., Salvatella X; Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Spain.; Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain., Garcia-Parajo MF; ICFO-Institut de Ciencies Fotoniques, The Barcelona Institute of Science and Technology, Barcelona, Spain.; Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain., Campelo F; ICFO-Institut de Ciencies Fotoniques, The Barcelona Institute of Science and Technology, Barcelona, Spain.
Jazyk:	angličtina
Zdroj:	ELife [Elife] 2024 Mar 11; Vol. 12. Date of Electronic Publication: 2024 Mar 11.
DOI:	10.7554/eLife.91708
Abstrakt:	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 Interests: PL, CG, YW, JV, CR, HS, VM, MG No competing interests declared, XS founder and scientific advisor of Nuage Therapeutics, FC Senior editor, eLife (© 2023, Lujan et al.)
Databáze:	MEDLINE
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