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. 2021 Mar 15;9:626095. doi: 10.3389/fcell.2021.626095

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Copyright © 2021 Rudd.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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p56^lck regulates the function of immune adaptors and CD28 co-stimulation. (A) p56^lck and related p59^fyn phosphorylate immune specific adaptors or molecular scaffolds. These include LAT, SLP-76, VAV, ADAP, and SKAP1. The C-terminal SH2 domain SLP-76 binds to the ADAP, while ADAP binds to SKAP1. (B) p56^lck and p59^fyn phosphorylate the cytoplasmic tail of CD28 YxxM site for the binding of PI 3K and GRB-2/ SOS. CD28 also have a more distal YAPP site which when phosphorylated, binds to the SH2 domain of p56^lck. The V3 domain of PKC-θ, in turn, binds to CD28 via binding to Lck. CD28 and PKCθ co-localize and act as markers for the c-SMAC.