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• W1566581202 abstract "Research Article15 November 1996free access Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. K. Salim K. Salim Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. J. Bottomley M. J. Bottomley Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author E. Querfurth E. Querfurth Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. J. Zvelebil M. J. Zvelebil Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author I. Gout I. Gout Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Scaife R. Scaife Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. L. Margolis R. L. Margolis Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Gigg R. Gigg Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author C. I. Smith C. I. Smith Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author P. C. Driscoll P. C. Driscoll Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. D. Waterfield M. D. Waterfield Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author G. Panayotou G. Panayotou Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author K. Salim K. Salim Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. J. Bottomley M. J. Bottomley Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author E. Querfurth E. Querfurth Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. J. Zvelebil M. J. Zvelebil Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author I. Gout I. Gout Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Scaife R. Scaife Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. L. Margolis R. L. Margolis Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Gigg R. Gigg Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author C. I. Smith C. I. Smith Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author P. C. Driscoll P. C. Driscoll Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author M. D. Waterfield M. D. Waterfield Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author G. Panayotou G. Panayotou Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author Author Information K. Salim1, M. J. Bottomley1, E. Querfurth1, M. J. Zvelebil1, I. Gout1, R. Scaife1, R. L. Margolis1, R. Gigg1, C. I. Smith1, P. C. Driscoll1, M. D. Waterfield1 and G. Panayotou1 1Ludwig Institute for Cancer Research, London, UK. The EMBO Journal (1996)15:6241-6250https://doi.org/10.1002/j.1460-2075.1996.tb01014.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Pleckstrin homology (PH) domains may act as membrane localization modules through specific interactions with phosphoinositide phospholipids. These interactions could represent responses to second messengers, with scope for regulation by soluble inositol polyphosphates. A biosensor-based assay was used here to probe interactions between PH domains and unilamellar liposomes containing different phospholipids and to demonstrate specificity for distinct phosphoinositides. The dynamin PH domain specifically interacted with liposomes containing phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] and, more weakly, with liposomes containing phosphatidylinositol-4-phosphate [PI(4)P]. This correlates with phosphoinositide activation of the dynamin GTPase. The functional GTPase of a dynamin mutant lacking the PH domain, however, cannot be activated by PI(4,5)P2. The phosphoinositide-PH domain interaction can be abolished selectively by point mutations in the putative binding pocket predicted by molecular modelling and NMR spectroscopy. In contrast, the Bruton's tyrosine kinase (Btk)PH domain specifically bound liposomes containing phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3]: an interaction requiring Arg28, a residue found to be mutated in some X-linked agammaglobulinaemia patients. A rational explanation for these different specificities is proposed through modelling of candidate binding pockets and is supported by NMR spectroscopy. Previous ArticleNext Article Volume 15Issue 221 November 1996In this issue RelatedDetailsLoading ..." @default.
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• W1566581202 title "Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase." @default.
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• W1566581202 doi "https://doi.org/10.1002/j.1460-2075.1996.tb01014.x" @default.
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