HIV-tat protein forms phosphoinositide-dependent membrane pores implicated in unconventional protein secretion
HIV-Tat has been demonstrated to be secreted from cells in a phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-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 β sheet...
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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
July 16, 2015
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| In: |
The journal of biological chemistry
Year: 2015, Volume: 290, Issue: 36, Pages: 21976-21984 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M115.667097 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M115.667097 Verlag, lizenzpflichtig, Volltext: http://www.jbc.org/content/290/36/21976 
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| Author Notes: | Marcel Zeitler, Julia P. Steringer, Hans-Michael Müller, Matthias P. Mayer, and Walter Nickel |
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| 520 | |a HIV-Tat has been demonstrated to be secreted from cells in a phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-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 β 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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