Journal
COMMUNICATIONS BIOLOGY
Volume 3, Issue 1, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/s42003-020-0871-y
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Funding
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [TRR 186, 278001972, TRR 83, Ni 423/7-1]
- DFG Cluster of Excellence CellNetworks at Heidelberg University
- Academy of Finland (Center of Excellence program)
- Helsinki Institute of Life Science (HiLIFE)
- Sigrid Juselius Foundation
- HPC-Europa3 Transnational Access program [HPC175W35X]
- DFG
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FGF2 is a tumor cell survival factor that is exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein secretion is based on direct translocation of FGF2 across the plasma membrane. The Na,K-ATPase has previously been shown to play a role in this process, however, the underlying mechanism has remained elusive. Here, we define structural elements that are critical for a direct physical interaction between FGF2 and the alpha 1 subunit of the Na,K-ATPase. In intact cells, corresponding FGF2 mutant forms were impaired regarding both recruitment at the inner plasma membrane leaflet and secretion. Ouabain, a drug that inhibits both the Na,K-ATPase and FGF2 secretion, was found to impair the interaction of FGF2 with the Na,K-ATPase in cells. Our findings reveal the Na,K-ATPase as the initial recruitment factor for FGF2 at the inner plasma membrane leaflet being required for efficient membrane translocation of FGF2 to cell surfaces.
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