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• W73166056 abstract "Research Article15 April 1996free access Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. B. Stahl B. Stahl Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author J. H. Chou J. H. Chou Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author C. Li C. Li Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author T. C. Südhof T. C. Südhof Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author R. Jahn R. Jahn Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author B. Stahl B. Stahl Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author J. H. Chou J. H. Chou Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author C. Li C. Li Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author T. C. Südhof T. C. Südhof Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author R. Jahn R. Jahn Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. Search for more papers by this author Author Information B. Stahl1, J. H. Chou1, C. Li1, T. C. Südhof1 and R. Jahn1 1Department of Pharmacology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA. The EMBO Journal (1996)15:1799-1809https://doi.org/10.1002/j.1460-2075.1996.tb00529.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info GTP activates the interaction between the synaptic vesicle proteins rabphilin and rab3. This raises the question of whether rabphilin is a resident vesicle protein that recruits rab3 in a stage-dependent fashion, or if it is instead an effector protein recruited by rab3. We now show that rabphilin, like rab3, dissociates from synaptic vesicles after exocytosis in a manner requiring both Ca2+ and membrane fusion. Rabphilin interacts with GTP-rab3 via a N-terminal domain comprising a novel Zn2+(-)finger motif, and this interaction is essential for rabphilin binding to synaptic vesicles. Thus, in the same way that ras recruits raf to the plasma membrane, rab3 reversibly recruits rabphilin to synaptic vesicles in a stage-dependent manner. These results reveal an unexpected similarity between the molecular mechanisms by which small G protein function in recruiting effector proteins to membranes during membrane traffic and signal transduction. Previous ArticleNext Article Volume 15Issue 81 April 1996In this issue RelatedDetailsLoading ..." @default.
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• W73166056 date "1996-04-01" @default.
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• W73166056 title "Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras." @default.
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• W73166056 doi "https://doi.org/10.1002/j.1460-2075.1996.tb00529.x" @default.
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