| |  Online-Ressource |
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| Verfasst von: | Zeitler, Marcel [VerfasserIn]  |
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| | Steringer, Julia Pauline [VerfasserIn] |
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| | Müller, Hans-Michael [VerfasserIn] |
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| | Mayer, Matthias P. [VerfasserIn] |
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| | Nickel, Walter [VerfasserIn] |
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| Titel: | HIV-tat protein forms phosphoinositide-dependent membrane pores implicated in unconventional protein secretion |
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| Verf.angabe: | Marcel Zeitler, Julia P. Steringer, Hans-Michael Müller, Matthias P. Mayer, and Walter Nickel |
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| E-Jahr: | 2015 |
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| Jahr: | July 16, 2015 |
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| Umfang: | 9 S. |
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| Fussnoten: | Gesehen am 21.07.2020 |
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| Titel Quelle: | Enthalten in: The journal of biological chemistry |
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| Ort Quelle: | Bethesda, Md. : Soc., 1905 |
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| Jahr Quelle: | 2015 |
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| Band/Heft Quelle: | 290(2015), 36, Seite 21976-21984 |
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| ISSN Quelle: | 1083-351X |
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| Abstract: | 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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| DOI: | doi:10.1074/jbc.M115.667097 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1074/jbc.M115.667097 |
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| | Volltext: http://www.jbc.org/content/290/36/21976 |
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| | DOI: https://doi.org/10.1074/jbc.M115.667097 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | FGF |
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| | FGF2 and membrane translocation |
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| | HIV-Tat |
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| | membrane bilayer |
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| | membrane lipid |
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| | membrane reconstitution |
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| | membrane recruitment and pore formation |
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| | phosphoinositide PI(4,5)P2 |
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| | plasma membrane |
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| | unconventional protein secretion |
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| K10plus-PPN: | 1725234521 |
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| Verknüpfungen: | → Zeitschrift |
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HIV-tat protein forms phosphoinositide-dependent membrane pores implicated in unconventional protein secretion / Zeitler, Marcel [VerfasserIn]; July 16, 2015 (Online-Ressource)
