Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 33, Pages 27659-27669Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.381939
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Funding
- German Research Foundation [SFB 638, GRK 1188]
- EuroMembrane Program of the European Science Foundation
- AID-NET Program of the Federal Ministry for Education and Research of Germany
- Deutsche Forschungsgemeinschaft cluster of excellence CellNetworks
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Fibroblast growth factor 2 (FGF2) is a critical mitogen with a central role in specific steps of tumor-induced angiogenesis. It is known to be secreted by unconventional means bypassing the endoplasmic reticulum/Golgi-dependent secretory pathway. However, the mechanism of FGF2 membrane translocation into the extracellular space has remained elusive. Here, we show that phosphatidylinositol 4,5-bisphosphate-dependent membrane recruitment causes FGF2 to oligomerize, which in turn triggers the formation of a lipidic membrane pore with a putative toroidal structure. This process is strongly up-regulated by tyrosine phosphorylation of FGF2. Our findings explain key requirements of FGF2 secretion from living cells and suggest a novel self-sustained mechanism of protein translocation across membranes with a lipidic membrane pore being a transient translocation intermediate.
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