Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region
Abstract 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 SK...
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doaj-12221994293d47f7924ee5903410045f2020-11-25T01:23:27ZengBMCBMC Research Notes1756-05002018-12-011111510.1186/s13104-018-3976-3Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal regionMonika Raab0Klaus Strebhardt1Christopher E. Rudd2Department of Obstetrics and Gynaecology, School of Medicine, J.W. Goethe-UniversityDepartment of Obstetrics and Gynaecology, School of Medicine, J.W. Goethe-UniversityDepartment of Obstetrics and Gynaecology, School of Medicine, J.W. Goethe-UniversityAbstract 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.http://link.springer.com/article/10.1186/s13104-018-3976-3SKAP1T-cellsDimerRapL |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Monika Raab Klaus Strebhardt Christopher E. Rudd |
spellingShingle |
Monika Raab Klaus Strebhardt Christopher E. Rudd Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region BMC Research Notes SKAP1 T-cells Dimer RapL |
author_facet |
Monika Raab Klaus Strebhardt Christopher E. Rudd |
author_sort |
Monika Raab |
title |
Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region |
title_short |
Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region |
title_full |
Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region |
title_fullStr |
Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region |
title_full_unstemmed |
Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region |
title_sort |
immune adaptor protein skap1 (skap-55) forms homodimers as mediated by the n-terminal region |
publisher |
BMC |
series |
BMC Research Notes |
issn |
1756-0500 |
publishDate |
2018-12-01 |
description |
Abstract 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. |
topic |
SKAP1 T-cells Dimer RapL |
url |
http://link.springer.com/article/10.1186/s13104-018-3976-3 |
work_keys_str_mv |
AT monikaraab immuneadaptorproteinskap1skap55formshomodimersasmediatedbythenterminalregion AT klausstrebhardt immuneadaptorproteinskap1skap55formshomodimersasmediatedbythenterminalregion AT christophererudd immuneadaptorproteinskap1skap55formshomodimersasmediatedbythenterminalregion |
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