Fam20C regulates protein secretion by Cab45 phosphorylation
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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.
Originalsprog | Engelsk |
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Tidsskrift | The Journal of Cell Biology |
Vol/bind | 219 |
Udgave nummer | 6 |
ISSN | 0021-9525 |
DOI | |
Status | Udgivet - 1 jun. 2020 |
Eksternt udgivet | Ja |
ID: 243474795