Fam20C regulates protein secretion by Cab45 phosphorylation

Tobias Karl Heinz Hecht, Birgit Blank, Martin Steger, Victor Lopez, Gisela Beck, Bulat Ramazanov, Matthias Mann, Vincent Tagliabracci, Julia Von Blume

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish (US)
Article numbere201910089
JournalJournal of Cell Biology
Volume219
Issue number6
DOIs
StatePublished - May 18 2020

ASJC Scopus subject areas

  • Cell Biology

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