Journal
DEVELOPMENTAL CELL
Volume 47, Issue 4, Pages 464-+Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2018.10.012
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Funding
- National Institute of General Medical Sciences of the United States National Institutes of Health [GM095766, GM060221, T32GM007223]
- Plus3 Perspective Program (Boehringer Ingelheim Foundation) [CRC914 (TP A09)]
- Deutsche Forschungsgemeinschaft (DFG) [BL 1186/4-1]
- Max Planck Institute of Biochemistry
- NIH-NCI Cancer Center Support Grant [P30 CA016059]
- US National Institutes of Health [S10RR031535]
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How the principal functions of the Golgi apparatus-protein processing, lipid synthesis, and sorting of macromolecules-are integrated to constitute cargo-specific trafficking pathways originating from the trans-Golgi network (TGN) is unknown. Here, we show that the activity of the Golgi localized SPCA1 calcium pump couples sorting and export of secreted proteins to synthesis of new lipid in the TGN membrane. A secreted Ca2+-binding protein, Cab45, constitutes the core component of a Ca2+-dependent, oligomerization-driven sorting mechanism whereby secreted proteins bound to Cab45 are packaged into a TGN-derived vesicular carrier whose membrane is enriched in sphingomyelin, a lipid implicated in TGN-to-cell surface transport. SPCA1 activity is controlled by the sphingomyelin content of the TGN membrane, such that local sphingomyelin synthesis promotes Ca2+ flux into the lumen of the TGN, which drives secretory protein sorting and export, thereby establishing a protein-and lipid-specific secretion pathway.
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