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. 2019 Sep 16;294(52):19852–19861. doi: 10.1074/jbc.RA119.009931

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© 2019 Lauenstein et al.

Author's Choice—Final version open access under the terms of the Creative Commons CC-BY license.

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Figure 7. — Constitutive SH3 domain interactions facilitate rapid SH2 domain binding upon BCAP tyrosine phosphorylation. Stepwise binding model for the SH2 and SH3 domain-containing BCAP-interaction partners p85 and PLC-γ2. The PI3K p85 or PLC-γ2 SH3 domains constitutively interact with BCAP proline-rich regions (Pro). The preformed complex can then rapidly engage in N-SH2 domain interaction upon BCAP tyrosine phosphorylation. High-affinity N-SH2 interactions facilitate the binding of lower-affinity C-SH2 domain interaction resulting in full activation of PI3K and PLC-γ2.