期刊
JOURNAL OF CELL BIOLOGY
卷 213, 期 3, 页码 305-314出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201601089
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资金
- Emmy Noether Fellowship [BL 1186/1-1]
- Deutsche Forschungsgemeinschaft [CRC914, SFB1035]
- FP7 Marie Curie Career Reintegration Grant
- Max Planck Institute of Biochemistry
- department of Molecular Medicine of Reinhard Fassler
- Center for NanoScience Munich
- Excellence Clusters Nanosystems Initiative Munich
- Center for integrated Protein Science Munich
Sorting and export of transmembrane cargoes and lysosomal hydrolases at the trans-Golgi network (TGN) are well understood. However, elucidation of the mechanism by which secretory cargoes are segregated for their release into the extracellular space remains a challenge. We have previously demonstrated that, in a reaction that requires Ca2+., the soluble TGN-resident protein Cab45 is necessary for the sorting of secretory cargoes at the TGN. Here, we report that Cab45 reversibly assembles into oligomers in the presence of Ca2+. These Cab45 oligomers specifically bind secretory proteins, such as COMP and LyzC, in a Ca2+-dependent manner in vitro. In intact cells, mutation of the Ca(2+-)binding sites in Cab45 impairs oligomerization, as well as COMP and LyzC sorting. Superresolution microscopy revealed that Cab45 colocalizes with secretory proteins and the TGN Ca2+ pump (SPCA1) in specific TGN microdomains. These findings reveal that Ca2+-dependent changes in Cab45 mediate sorting of specific cargo molecules at the TGN.
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