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

  • 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.

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Author:Monika RaabORCiD, Klaus StrebhardtORCiD, Christopher E. Rudd
Pubmed Id:
Parent Title (English):BMC Research Notes
Publisher:Biomed Central
Place of publication:London
Document Type:Article
Year of Completion:2018
Date of first Publication:2018/12/06
Publishing Institution:Universit├Ątsbibliothek Johann Christian Senckenberg
Release Date:2019/05/27
Tag:Dimer; RapL; SKAP1; T-cells
Issue:1, Art. 869
Page Number:5
First Page:1
Last Page:5
Open Access: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( applies to the data made available in this article, unless otherwise stated.
Institutes:Medizin / Medizin
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Licence (German):License LogoCreative Commons - Namensnennung 4.0