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. 2019 Sep 4;294(42):15480–15494. doi: 10.1074/jbc.RA119.008318

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© 2019 Andersen et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 8. — Schematic representation of TSAD-ITK-LCK interactions and their putative sequence. A, open LCK binds to TSAD PRR and becomes activated. B, active LCK phosphorylates the three TSAD C-terminal tyrosines. C, the LCK SH2 domain binds to TSAD pTyr, allowing LCK SH3 to detach from TSAD PRR. ITK binds to TSAD PRR. D, active LCK phosphorylates ITK Tyr⁵¹¹. E, active ITK pTyr⁵¹¹ autophosphorylates ITK Tyr¹⁸⁰. ITK pTyr¹⁸⁰ does not bind to TSAD PRR. F, active LCK remains bound to TSAD pTyr. Next, the ITK molecule (indicated in a different color) binds to TSAD PRR, and the process starts over from D.