Role of two modules controlling the interaction between SKAP1 and SRC kinases comparison with SKAP2 architecture and consequences for evolution

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Levillayer, Laurine | Brighelli, Camille | Demeret, Caroline | Sakuntabhai, Anavaj | Bureau, Jean-François

Edité par CCSD ; Public Library of Science -

International audience. SRC kinase associated phosphoprotein 1 (SKAP1), an adaptor for protein assembly, plays an important role in the immune system such as stabilizing immune synapses. Understand- ing how these functions are controlled at the level of the protein-protein interactions is nec- essary to describe these processes and to develop therapeutics. Here, we dissected the SKAP1 modular organization to recognize SRC kinases and compared it to that of its para- log SRC kinase associated phosphoprotein 2 (SKAP2). Different conserved motifs common to either both proteins or specific to SKAP2 were found using this comparison. Two modules harboring different binding properties between SKAP1 and SKAP2 were identified: one composed of two conserved motifs located in the second interdomain interacting at least with the SH2 domain of SRC kinases and a second one composed of the DIM domain mod- ulated by the SH3 domain and the activation of SRC kinases. This work suggests a conver- gent evolution of the binding properties of some SRC kinases interacting specifically with either SKAP1 or SKAP2.

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