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International Immunology Advance Access originally published online on September 29, 2007
International Immunology 2007 19(11):1313-1318; doi:10.1093/intimm/dxm100
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© The Japanese Society for Immunology. 2007. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Investigating the functional role of CD2BP2 in T cells

Matthias Heinze, Michael Kofler and Christian Freund

Protein Engineering Group, Leibniz-Institute of Molecular Pharmacology and Free University Berlin, Robert-Rössle-Strasse 10, 13125 Berlin, Germany

Correspondence to: C. Freund; E-mail: freund{at}fmp-berlin.de

The adaptor protein CD2-binding protein 2 (CD2BP2) confers binding to proline-rich sequences (PRS) via its GYF domain. In addition to the cytoplasmic domain of CD2, several other proteins were identified as interaction partners of CD2BP2, but the in vivo significance of these findings is unclear. We now show that CD2BP2’s nuclear localization is not changed when CD2 and CD2BP2 are co-expressed in HeLa cells, indicating that other PRS compete effectively for CD2BP2 binding in the nucleus. Since the CD2BP2-binding motifs of CD2 are known to be involved in cytokine signaling, we tested the effect of CD2BP2 knockdown in PBMCs on the expression of T-cell cytokines. No major difference in cytokine expression can be observed for primary cells transfected with CD2BP2-specific small interfering RNA. We conclude that CD2 signaling is at least partially independent of its in vitro binding partner CD2BP2.

Keywords: CD2, CD2BP2, cytokines, GYF, proline-rich sequences

Transmitting editor: S. Koyasu

Received 30 January 2007, accepted 4 September 2007.


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