[HTML][HTML] Regulation of the p85/p110α phosphatidylinositol 3′-kinase: distinct roles for the N-terminal and C-terminal SH2 domains
J Yu, C Wjasow, JM Backer - Journal of Biological Chemistry, 1998 - ASBMB
Our previous studies on the p85/p110α phosphatidylinositol 3-kinase showed that the p85
regulatory subunit inhibits the p110α catalytic subunit, and that phosphopeptide activation of
p85/p110α dimers reflects a disinhibition of p110α (Yu, J., Zhang, Y., McIlroy, J., Rordorf-
Nikolic, T., Orr, GA, and Backer, JM (1998) Mol. Cell. Biol. 18, 1379–1387). We now define
the domains of p85 required for inhibition of p110α. The iSH2 domain of p85 is sufficient to
bind p110α but does not inhibit it. Inhibition of p110α requires the presence of the nSH2 …
regulatory subunit inhibits the p110α catalytic subunit, and that phosphopeptide activation of
p85/p110α dimers reflects a disinhibition of p110α (Yu, J., Zhang, Y., McIlroy, J., Rordorf-
Nikolic, T., Orr, GA, and Backer, JM (1998) Mol. Cell. Biol. 18, 1379–1387). We now define
the domains of p85 required for inhibition of p110α. The iSH2 domain of p85 is sufficient to
bind p110α but does not inhibit it. Inhibition of p110α requires the presence of the nSH2 …