TY - JOUR
T1 - Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase
AU - Otsu, Masayuki
AU - Hiles, Ian
AU - Gout, Ivan
AU - Fry, Michael J.
AU - Ruiz-Larrea, Fernanda
AU - Panayotou, George
AU - Thompson, Andrew
AU - Dhand, Ritu
AU - Hsuan, Justin
AU - Totty, Nicholas
AU - Smith, Anthony D.
AU - Morgan, Sarah J.
AU - Courtneidge, Sara A.
AU - Parker, Peter J.
AU - Waterfield, Michael D.
N1 - Funding Information:
We would like to thank the following people for help and materials provided during the course of this work: Dr. R. Dixon (Merck, Sharp and Dohme, PA) for bovine brain cortex cDNA libraries; Dr. C. Heldin (Ludwig Institute, Uppsala Branch, Sweden) for porcine aortic endothelial cells overexpressing the human PDGF J~-receptor, COS-1 cells, and the pSV7d expression vector containing the human PDGF ~-receptor; Dr. C. George-Nascimento (Chiron Corp.) for the PDGF (BB homo-dimer); Dr. J. Brugge (University of Pennsylvania) for the pp60~~c; Dr. B. Griffin (Royal Postgraduate Medical School, Hammersmith, England) for the polyoma virus mT antigen baculovirus vectors; Dr. D. Melton (Harvard) for pSP64T vector; Dr. R. J. Kaufman (Genetics Institute) for the pMT-2 vector; Dr. G. StJ. Whitley (St. George's Hospital, London) for the bovine adrenal cortex cell line. Finally, we would like to thank Geoff Scrace for help with sequence analysis, Alistair Sterling for oligonucleotide and Oanh Nguyen for peptide synthesis, and Angelika Heber and Andrew Cartwright for technical assistance with the mT:pp60 ~'~c experiments. I. G. was supported by a grant from Imperial Chemical Industries during part of his work on this project. S. J. M. was supported by a grant from Glaxo Group Research.
PY - 1991/4/5
Y1 - 1991/4/5
N2 - Affinity-purified bovine brain phosphatidylinositol 3-kinase (PI3-kinase) contains two major proteins of 85 and 110 kd. Amino acid sequence analysis and cDNA cloning reveals two related 85 kd proteins (p85α and p85β), which both contain one SH3 and two SH2 regions (src homology regions). When expressed, these 85 kd proteins bind to and are substrates for tyrosine-phosphorylated receptor kinases and the polyoma virus middle-T antigen/pp60c-src complex, but lack PI3-kinase activity. However, an antiserum raised against p85β immunoprecipitates PI3-kinase activity. The active PI3-kinase complex containing p85α or p85β and the 110 kd protein binds to PDGF but not EGF receptors. p85α and p85β may mediate specific PI3-kinase interactions with a subset of tyrosine kinases.
AB - Affinity-purified bovine brain phosphatidylinositol 3-kinase (PI3-kinase) contains two major proteins of 85 and 110 kd. Amino acid sequence analysis and cDNA cloning reveals two related 85 kd proteins (p85α and p85β), which both contain one SH3 and two SH2 regions (src homology regions). When expressed, these 85 kd proteins bind to and are substrates for tyrosine-phosphorylated receptor kinases and the polyoma virus middle-T antigen/pp60c-src complex, but lack PI3-kinase activity. However, an antiserum raised against p85β immunoprecipitates PI3-kinase activity. The active PI3-kinase complex containing p85α or p85β and the 110 kd protein binds to PDGF but not EGF receptors. p85α and p85β may mediate specific PI3-kinase interactions with a subset of tyrosine kinases.
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U2 - 10.1016/0092-8674(91)90411-Q
DO - 10.1016/0092-8674(91)90411-Q
M3 - Article
C2 - 1707345
AN - SCOPUS:0025755422
SN - 0092-8674
VL - 65
SP - 91
EP - 104
JO - Cell
JF - Cell
IS - 1
ER -