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Fam20C regulates protein secretion by Cab45 phosphorylation

MPS-Authors
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Hecht,  Tobias Karl-Heinz
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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Blank,  Birgit
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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Steger,  Martin
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Beck,  Gisela
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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Mann,  Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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von Blume,  Julia
von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Hecht, T.-K.-H., Blank, B., Steger, M., Lopez, V., Beck, G., Ramazanov, B., et al. (2020). Fam20C regulates protein secretion by Cab45 phosphorylation. JOURNAL OF CELL BIOLOGY, 219(6): e201910089. doi:10.1083/jcb.201910089.


Cite as: http://hdl.handle.net/21.11116/0000-0006-A385-B
Abstract
The TGN is a key compartment for the sorting and secretion of newly synthesized proteins. At the TGN, soluble proteins are sorted based on the instructions carried in their oligosaccharide backbones or by a Ca2+-mediated process that involves the cargo-sorting protein Cab45. Here, we show that Cab45 is phosphorylated by the Golgi-specific protein kinase Fam20C. Mimicking of phosphorylation translocates Cab45 into TGN-derived vesicles, which goes along with an increased export of LyzC, a Cab45 client. Our findings demonstrate that Fam20C plays a key role in the export of Cab45 clients by fine-tuning Cab45 oligomerization and thus impacts Cab45 retention in the TGN.