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Activation of Phosphatidylinositol-3′ Kinase by Src-Family Kinase SH3 Binding to the p85 Subunit

Pleiman, Christopher M., Hertz, W. Marc, Cambier, John C.·1994·Science

Abstract

Engagement of antigen receptor complexes induces rapid activation of Src-family kinases and association with phosphatidylinositol-3′ kinase (PI-3 kinase). Here it was found that the Src homology 3 (SH3) domain of Lyn and Fyn bound to a proline-rich region (residues 84 to 99) within the 85-kilodalton subunit (p85) of PI-3 kinase. The binding of SH3 to the purified kinase led to a five- to sevenfold increase in the specific activity of PI-3 kinase. Ligand-induced receptor stimulation activated PI-3 kinase, and this activation was blocked by a peptide containing residues 84 to 99 of p85. These data demonstrate a mechanism for PI-3 kinase activation and show that binding of SH3 domains to proline-rich target sequences can regulate enzymatic activity.

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Metadata

Authors
Pleiman, C. M., Hertz, W. M., & Cambier, J. C.
Venue
Science
Published
1994-03-18
Volume
263
Issue
5153
Pages
1609-1612
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1979187651
Cited by
436
References
0
FWCI
18.14
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Activation of Phosphatidylinositol-3′ Kinase by Src-Family Kinase SH3 Binding to the p85 Subunit. https://app.cochat.ai/papers/10.1126/science.8128248
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Pleiman, C. M., Hertz, W. M., & Cambier, J. C. (1994). Activation of Phosphatidylinositol-3′ Kinase by Src-Family Kinase SH3 Binding to the p85 Subunit. Science. https://doi.org/10.1126/science.8128248

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