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A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system.

1995; Springer Nature; Volume: 14; Issue: 14 Linguagem: Inglês

10.1002/j.1460-2075.1995.tb07340.x

1460-2075

Stefano Volinia, Ritu Dhand, Bart Vanhaesebroeck, Lindsay K. MacDougall, Robert C. Stein, Marketa Zvelebil, J. Domin, Christina Panaretou, Michael D. Waterfield,

Protein Kinase Regulation and GTPase Signaling

Research Article17 July 1995free access A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. S. Volinia S. Volinia Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Dhand R. Dhand Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author B. Vanhaesebroeck B. Vanhaesebroeck Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author L.K. MacDougall L.K. MacDougall Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Stein R. Stein 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 J. Domin J. Domin Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author C. Panaretou C. Panaretou 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 S. Volinia S. Volinia Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Dhand R. Dhand Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author B. Vanhaesebroeck B. Vanhaesebroeck Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author L.K. MacDougall L.K. MacDougall Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author R. Stein R. Stein 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 J. Domin J. Domin Ludwig Institute for Cancer Research, London, UK. Search for more papers by this author C. Panaretou C. Panaretou 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 Author Information S. Volinia1, R. Dhand1, B. Vanhaesebroeck1, L.K. MacDougall1, R. Stein1, M.J. Zvelebil1, J. Domin1, C. Panaretou1 and M.D. Waterfield1 1Ludwig Institute for Cancer Research, London, UK. The EMBO Journal (1995)14:3339-3348https://doi.org/10.1002/j.1460-2075.1995.tb07340.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Phosphoinositide (PI) 3-kinases have been characterized as enzymes involved in receptor signal transduction in mammalian cells and in a complex which mediates protein trafficking in yeast. PI 3-kinases linked to receptors with intrinsic or associated tyrosine kinase activity are heterodimeric proteins, consisting of p85 adaptor and p110 catalytic subunits, which can generate the 3-phosphorylated forms of phosphatidylinositol (PtdIns), PtdIns4P and PtdIns(4,5)P2 as potential second messengers. Yeast Vps34p kinase, however, has a substrate specificity restricted to PtdIns and is a PtdIns 3-kinase. Here the molecular characterization of a new human PtdIns 3-kinase with extensive sequence homology to Vps34p is described. PtdIns 3-kinase does not associate with p85 and phosphorylates PtdIns, but not PtdIns4P or PtdIns(4,5)P2. In vivo PtdIns 3-kinase is in a complex with a cellular protein of 150 kDa, as detected by immunoprecipitation from human cells. Protein sequence analysis and cDNA cloning show that this 150 kDa protein is highly homologous to Vps15p, a 160 kDa protein serine/threonine kinase associated with yeast Vps34p. These results suggest that the major components of the yeast Vps intracellular trafficking complex are conserved in humans. Previous ArticleNext Article Volume 14Issue 141 July 1995In this issue RelatedDetailsLoading ...