期刊
JOURNAL OF CELL BIOLOGY
卷 219, 期 6, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201910089
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资金
- Deutsche Forschungsgemeinschaft Perspective Program (Boehringer Ingelheim Foundation) [BL 1186/4-1]
- National Institutes of Health National Institute of General Medical Sciences [GM134083-01]
- Welch Foundation [I-1911]
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.
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