TY - JOUR
T1 - Fam20C regulates protein secretion by Cab45 phosphorylation
AU - Hecht, Tobias Karl Heinz
AU - Blank, Birgit
AU - Steger, Martin
AU - Lopez, Victor
AU - Beck, Gisela
AU - Ramazanov, Bulat
AU - Mann, Matthias
AU - Tagliabracci, Vincent
AU - Von Blume, Julia
N1 - Funding Information:
J. von Blume was funded by the Deutsche Forschungsgemeinschaft Perspective Program (Boehringer Ingelheim Foundation; project grant BL 1186/4-1) and the National Institutes of Health National Institute of General Medical Sciences (award number GM134083-01). V. Tagliabracci was funded by the Welch Foundation (grant I-1911).
Funding Information:
J. von Blume was funded by the Deutsche Forschungsgemeinschaft Perspective Program (Boehringer Ingelheim Foundation; project grant BL 1186/4-1) and the National Institutes of Health National Institute of General Medical Sciences (award number GM134083-01). V. Tagliabracci was funded by the Welch Foundation (grant I-1911). The authors declare no competing financial interests.
Publisher Copyright:
© 2020 Hecht et al.
PY - 2020/5/18
Y1 - 2020/5/18
N2 - 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.
AB - 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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U2 - 10.1083/JCB.201910089
DO - 10.1083/JCB.201910089
M3 - Article
C2 - 32422653
AN - SCOPUS:85084785406
SN - 0021-9525
VL - 219
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 6
M1 - e201910089
ER -