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 |
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| Rok vydání: | 1992 |
| Předmět: |
Insecta
animal structures receptor Protein subunit Molecular Sequence Data Lipid kinase activity Receptor Macrophage Colony-Stimulating Factor Signal transduction Biology Polymerase Chain Reaction Catalysis General Biochemistry Genetics and Molecular Biology Receptor tyrosine kinase Cell Line Phosphatidylinositol 3-Kinases chemistry.chemical_compound Sequence Homology Nucleic Acid Complementary DNA cancer Animals Amino Acid Sequence RNA Messenger Phosphatidylinositol Cloning Molecular Base Sequence Phospholipase C Kinase Phosphotransferases Protein primary structure tyrosine kinase Brain DNA Precipitin Tests Blotting Southern Biochemistry chemistry embryonic structures biology.protein Cattle |
| Zdroj: | Cell. 70:419-429 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/0092-8674(92)90166-a |
| Popis: | 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 tyrosine kinases. Here the characterization of the p110 subunit is presented. cDNA cloning reveals p110 to be a 1068 aa protein related to Vps34p, a S. cerevisiae protein involved in the sorting of proteins to the vacuole. p110 expressed in insect cells possesses Pl3-kinase activity and associates with p85 alpha into an active p85 alpha-p110 complex that binds the activated colony-stimulating factor 1 receptor. p110 expressed in COS-1 cells is catalytically active only when complexed with p85 alpha. |
| Databáze: | OpenAIRE |
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