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Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region.


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Raab, Monika 
Strebhardt, Klaus 
Rudd, Christopher E  ORCID logo


OBJECTIVE: Immune cell adaptor protein SKAP1 couples the antigen-receptor (TCR/CD3) with the activation of LFA-1 adhesion in T-cells. Previous work by ourselves and others have shown that SKAP1 can directly bind to other adaptors such as ADAP and RapL. However, it has been unclear whether SKAP1 can form homodimers with itself and the regions within SKAP1 that mediated homodimer formation. RESULTS: Here, we show that SKAP1 and SKAP2 form homodimers in cells. Homodimer formation of immune adaptor protein SKAP1 (SKAP-55) are mediated by residues A17 to L21 in the SKAP1 N-terminal region. SKAP1 dimer formation was not needed for its binding to RapL. These data indicate that the pathway linking SKAP1 to RapL is not dependent on the homo-dimerization of SKAP1.



Dimer, RapL, SKAP1, T-cells, Humans, Phosphoproteins, Protein Binding, Protein Multimerization, Reproducibility of Results, rap1 GTP-Binding Proteins

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