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- W2059307851 abstract "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." @default.
- W2059307851 created "2016-06-24" @default.
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- W2059307851 date "2012-08-01" @default.
- W2059307851 modified "2023-10-07" @default.
- W2059307851 title "Phosphatidylinositol 4,5-Bisphosphate (PI(4,5)P2)-dependent Oligomerization of Fibroblast Growth Factor 2 (FGF2) Triggers the Formation of a Lipidic Membrane Pore Implicated in Unconventional Secretion" @default.
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- W2059307851 doi "https://doi.org/10.1074/jbc.m112.381939" @default.
- W2059307851 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3431657" @default.
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