Fam20C regulates protein secretion by Cab45 phosphorylation
Fam20C regulates protein secretion by Cab45 phosphorylation
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DOI：
10.1083/jcb.201910089
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发表时间：
2020-06-01
影响因子：
7.8
通讯作者：
von Blume, Julia
中科院分区：
文献类型：
--
作者：
Hecht, Tobias Karl-Heinz;Blank, Birgit;von Blume, Julia
TGN是新合成蛋白质的分选和分泌的关键隔室。在TGN，可溶性蛋白质根据其寡糖骨架中携带的指令或通过涉及货物分选蛋白Cab45的Ca2+介导的过程进行分选。在这里，我们表明，Cab45被高尔基体特异性蛋白激酶Fam20C磷酸化。模拟磷酸化使Cab45易位到TGN衍生的囊泡中，这沿着增加的LyzC（Cab45客户端）输出。我们的研究结果表明，Fam20C通过微调Cab45寡聚化在Cab45客户端的出口中起着关键作用，从而影响Cab45在TGN中的保留。
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.