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Cloning and Characterization of a G Protein-Activated Human Phosphoinositide-3 Kinase

Autor: Ignacio Rubio, J. Justin Hsuan, Peter Gierschik, Michael Loubtchenkov, Theodor Hanck, Ritu Dhand, Bernd Nürnberg, Klaus Seedorf, Borislav Stoyanov, Michael D. Waterfield, Reinhard Wetzker, Stefka Stoyanova, Stefano Volinia, Daria Malek, Bart Vanhaesebroeck

Publikováno v: Science. 269:690-693

Phosphoinositide-3 kinase activity is implicated in diverse cellular responses triggered by mammalian cell surface receptors and in the regulation of protein sorting in yeast. Receptors with intrinsic and associated tyrosine kinase activity recruit h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da292551b50e65163cb631b9c2b18786
https://doi.org/10.1126/science.7624799

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Biochemical characterization of the free catalytic p110 alpha and the complexed heterodimeric p110 alpha.p85 alpha forms of the mammalian phosphatidylinositol 3-kinase

Autor: Peter J. Parker, Michael J. Fry, Ritu Dhand, Ruediger Woscholski, Mike Waterfield

Publikováno v: Journal of Biological Chemistry. 269:25067-25072

The regulatory (p85 alpha) and catalytic (p110 alpha) subunits of the mammalian phosphatidylinositol 3-kinase have been expressed in insect cells using the baculovirus sytem. The free catalytic subunit p110 alpha and the coexpressed heterodimeric com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5577662c10c66b0553e41a285a1ce659
https://doi.org/10.1016/s0021-9258(17)31499-0

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The catalytic subunit of phosphatidylinositol 3-kinase is a substrate for the activated platelet-derived growth factor receptor, but not for middle-T antigen-pp60c-src complexes

Autor: Sara A. Courtneidge, Serge Roche, Mike Waterfield, Ritu Dhand

Publikováno v: Biochemical Journal. 301:703-711

The interaction of phosphatidylinositol 3-kinase (PI 3-K) with polyoma-virus middle-T antigen-pp60c-src (mT:cSrc) complexes and with the platelet-derived growth factor (PDGF) receptor has been investigated. Firstly, we undertook reconstitution studie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6409ae4045451385816100d9abb1527
https://doi.org/10.1042/bj3010703

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PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity

Autor: George Panayotou, Serge Roche, P Vicendo, Michael J. Fry, Ritu Dhand, Nick Totty, Ivan Gout, Ian Hiles, K. Yonezawa, Oanh Truong

Publikováno v: The EMBO Journal. 13:522-533

Phosphatidylinositol 3-kinase (PI 3-kinase) has a regulatory 85 kDa adaptor subunit whose SH2 domains bind phosphotyrosine in specific recognition motifs, and a catalytic 110 kDa subunit. Mutagenesis of the p110 subunit, within a sequence motif commo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::717eda3b305db5cf9d20ef53c1b64af2
https://doi.org/10.1002/j.1460-2075.1994.tb06290.x

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The GTPase dynamin binds to and is activated by a subset of SH3 domains

Autor: Michael J. Fry, Iain D. Campbell, Oanh Truong, Ian Hiles, Nicholas F. Totty, George Panayotou, Ivan Gout, Michael D. Waterfield, J. Justin Hsuan, Ritu Dhand, Grant W. Booker, Pamela Das

Publikováno v: Cell. 75:25-36

Summary Src homology 3 (SH3) domains have been implicated in mediating protein-protein interactions in receptor signaling processes; however, the precise role of this domain remains unclear. In this report, affinity purification techniques were used

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8da96c91a8a75f91fd5eeea3edddbed5
https://doi.org/10.1016/s0092-8674(05)80081-9

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Purification and characterization of a phosphatidylinositol 3-kinase complex from bovine brain by using phosphopeptide affinity columns

Autor: Sara A. Courtneidge, George Panayotou, Ivan Gout, Fernanda Ruiz-Larrea, O Nguyen, Ritu Dhand, Michael J. Fry, Mike Waterfield

Publikováno v: Biochemical Journal. 288:383-393

Specific phosphorylated tyrosine residues in the kinase insert region of the human platelet-derived-growth-factor beta-receptor mediate the formation of multienzyme complexes with this receptor. When phosphorylated, tyrosine residue 751 within the ki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cf0c06a295f286a3198b1362e4cb751
https://doi.org/10.1042/bj2880383

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Phosphatidylinositol 3-kinase: Structure and expression of the 110 kd catalytic subunit

Autor: Sara A. Courtneidge, Nicholas F. Totty, Fernanda Ruiz-Larrea, Andrew J. Thompson, Ian Hiles, Stefano Volinia, Ritu Dhand, George Panayotou, J. Justin Hsuan, Peter J. Parker, Michael D. Waterfield, Ivan Gout, Masayuki Otsu, Michael J. Fry

Publikováno v: Cell. 70:419-429

Purified bovine brain phosphatidylinositol 3-kinase (Pl3-kinase) is composed of 85 kd and 110 kd subunits. The 85 kd subunit (p85 alpha) lacks Pl3-kinase activity and acts as an adaptor, coupling the 110 kd subunit (p110) to activated protein tyrosin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4d8efadf704ae508a5d5d367a704f77
https://doi.org/10.1016/0092-8674(92)90166-a

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