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Dominant negative effect of the truncated p110 subunit of phosphatidylinositol‐3 kinase
Author(s) -
Takayanagi Junji,
Kimura Koutarou,
Nishioka Naoya,
Akimoto Kazunori,
Moriya Shigeharu,
Ohno Shigeo,
Fukui Yasuhisa
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201801
Subject(s) - p110α , protein subunit , mutant , phosphatidylinositol , pi , chemistry , signal transduction , kinase , microbiology and biotechnology , binding site , biology , biochemistry , gene
Effects of p110, the catalytic subunit of PI‐3 kinase, on induction of TPA response element‐driven promoter by EGF was examined. The induction was enhanced by co‐expression of the wild type p110. The truncated p110 mutants containing the binding site for p85 but missing the catalytic activity repressed the induction. A mutant with no binding activity to p85 did not show this effect. These results suggest that PI‐3 kinase is involved in signal transduction of EGF and that the truncated p110s capable of binding to p85 serves as a dominant negative reagent for PI‐3 kinase.