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PHOSPHATIDYLINOSITOL 3-KINASE - STRUCTURE AND EXPRESSION OF THE 110KD CATALYTIC SUBUNIT

HILES, ID; OTSU, M; VOLINIA, S; FRY, MJ; GOUT, I; DHAND, R; ... WATERFIELD, MD; + view all (1992) PHOSPHATIDYLINOSITOL 3-KINASE - STRUCTURE AND EXPRESSION OF THE 110KD CATALYTIC SUBUNIT. CELL , 70 (3) 419 - 429.

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Abstract

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.

Type:Article
Title:PHOSPHATIDYLINOSITOL 3-KINASE - STRUCTURE AND EXPRESSION OF THE 110KD CATALYTIC SUBUNIT
Keywords:RECEPTOR TYROSINE KINASES, DEPENDENT PROTEIN-KINASE, FACTOR-I RECEPTOR, MIDDLE T-ANTIGEN, PDGF RECEPTOR, BOVINE BRAIN, SACCHAROMYCES-CEREVISIAE, SIGNAL TRANSDUCTION, ACTIVATED NEUTROPHILS, PHOSPHOLIPASE-C

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