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Fam20C regulates protein secretion by Cab45 phosphorylation.


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.

SUBMITTER: Hecht TK 

PROVIDER: S-EPMC7265331 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

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Fam20C regulates protein secretion by Cab45 phosphorylation.

Hecht Tobias Karl-Heinz TK   Blank Birgit B   Steger Martin M   Lopez Victor V   Beck Gisela G   Ramazanov Bulat B   Mann Matthias M   Tagliabracci Vincent V   von Blume Julia J  

The Journal of cell biology 20200601 6


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 cl  ...[more]

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