期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 36, 页码 21976-21984出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M115.667097
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资金
- German Research Council [DFG-SFB 638, DFG-SFB/TRR 83, DFG-GRK1188]
- AID-NET program of the Federal Ministry for Education and Research of Germany
- cluster of excellence CellNetworks
HIV-Tat has been demonstrated to be secreted from cells in a phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2)-dependent manner. Here we show that HIV-Tat forms membrane-inserted oligomers, a process that is accompanied by changes in secondary structure with a strong increase in antiparallel beta sheet content. Intriguingly, oligomerization of HIV-Tat on membrane surfaces leads to the formation of membrane pores, as demonstrated by physical membrane passage of small fluorescent tracer molecules. Although membrane binding of HIV-Tat did not strictly depend on PI(4,5) P2 but, rather, was mediated by a range of acidic membrane lipids, a functional interaction between PI(4,5) P2 and HIV-Tat was critically required for efficient membrane pore formation by HIV-Tat oligomers. These properties are strikingly similar to what has been reported previously for fibroblast growth factor 2 (FGF2), providing strong evidence of a common core mechanism of unconventional secretion shared by HIV-Tat and fibroblast growth factor 2.
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