Immunogenetics

, Volume 58, Issue 1, pp 15–25

Identification and characterization of two related murine genes, Eat2a and Eat2b, encoding single SH2-domain adapters

Authors

    • Division of Immunology BIDMCHarvard Medical School
  • Erika Erdős
    • Institute of ImmunologyUniversity of Debrecen Medical and Health Science Center
  • Gongxian Liao
    • Division of Immunology BIDMCHarvard Medical School
  • Ninghai Wang
    • Division of Immunology BIDMCHarvard Medical School
  • Svend Rietdijk
    • Division of Immunology BIDMCHarvard Medical School
  • Maria Simarro
    • Division of Immunology BIDMCHarvard Medical School
  • Beata Scholtz
    • Department of Biochemistry and Molecular BiologyUniversity of Debrecen Medical and Health Science Center
  • Jill Mooney
    • Department of Pathology and Center for ImmunologyUniversity of Texas Southwestern Medical Center
  • Chang Hoon Lee
    • Laboratory of ImmunopathologyNational Institute of Allergy and Infectious Diseases
  • Min Sun Shin
    • Laboratory of ImmunopathologyNational Institute of Allergy and Infectious Diseases
  • Éva Rajnavölgyi
    • Institute of ImmunologyUniversity of Debrecen Medical and Health Science Center
  • John Schatzle
    • Department of Pathology and Center for ImmunologyUniversity of Texas Southwestern Medical Center
  • Herbert C. MorseIII
    • Laboratory of ImmunopathologyNational Institute of Allergy and Infectious Diseases
  • Cox Terhorst
    • Division of Immunology BIDMCHarvard Medical School
  • Arpad Lanyi
    • Institute of ImmunologyUniversity of Debrecen Medical and Health Science Center
Original Paper

DOI: 10.1007/s00251-005-0056-3

Cite this article as:
Calpe, S., Erdős, E., Liao, G. et al. Immunogenetics (2006) 58: 15. doi:10.1007/s00251-005-0056-3

Abstract

Human EAT-2 (SH2D1B) and SLAM-associated protein (SAP) (SH2D1A) are single SH2-domain adapters, which bind to specific tyrosine residues in the cytoplasmic tail of six signaling lymphocytic activation molecule (SLAM) (SLAMF1)-related receptors. Here we report that, unlike in humans, the mouse and rat Eat2 genes are duplicated with an identical genomic organization. The coding regions of the mouse Eat2a and Eat2b genes share 91% identity at the nucleotide level and 84% at the protein level; similarly, segments of introns are highly conserved. Whereas expression of mouse Eat2a mRNA was detected in multiple tissues, Eat2b was only detectable in mouse natural killer cells, CD8+ T cells, and ovaries, suggesting a very restricted tissue expression of the latter. Both the EAT-2A and EAT-2B coimmunoprecipitated with mouse SLAM in transfected cells and augmented tyrosine phosphorylation of the cytoplasmic tail of SLAM. Both EAT-2A and EAT-2B bind to the Src-like kinases Fyn, Hck, Lyn, Lck, and Fgr, as determined by a yeast two-hybrid assay. However, unlike SAP, the EAT-2 proteins bind to their kinase domains and not to the SH3 domain of these kinases. Taken together, the data suggest that both EAT-2A and EAT-2B are adapters that recruit Src kinases to SLAM family receptors using a mechanism that is distinct from that of SAP.

Keywords

Adapter proteinsEAT-2SLAMSrc kinases

Supplementary material

251_2005_56_MOESM1_ESM.ppt (22 kb)
Fig. S1Genomic organization of the Rat eat-2 genes (PPT 23KB)
251_2005_56_MOESM2_ESM.doc (36 kb)
Fig. S2Alignment of the amino acid sequences of EAT-2A and EAT-2B in different species and mouse strains (DOC 36KB)
251_2005_56_MOESM3_ESM.ppt (1.9 mb)
Fig. S3Expression of the mouse EAT-2 genes in several tumor B-cell lines (PPT 1MB)

Copyright information

© Springer-Verlag 2006