Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 May;87(9):3319–3323. doi: 10.1073/pnas.87.9.3319

Molecular cloning of the CD3 eta subunit identifies a CD3 zeta-related product in thymus-derived cells.

Y J Jin 1, L K Clayton 1, F D Howard 1, S Koyasu 1, M Sieh 1, R Steinbrich 1, G E Tarr 1, E L Reinherz 1
PMCID: PMC53891  PMID: 2139725

Abstract

The CD3 eta subunit of the T-cell antigen receptor forms a heterodimeric structure with the CD3 zeta subunit in thymus-derived lymphoid cells and is apparently involved in signal transduction through the receptor. Here we report the primary structure of murine CD3 eta as deduced from protein microsequencing and cDNA cloning. The mature protein is divided into three domains: a 9-amino acid extracellular segment, a 21-amino acid transmembrane segment including a negatively charged residue characteristic of CD3 subunits, and a 155-amino acid cytoplasmic tail. The NH2-terminal sequences of CD3 eta and CD3 zeta are identical through amino acid 122 of each mature protein but then diverge in the remainder of their respective COOH-terminal regions, consistent with alternatively spliced products of a common gene. The cytoplasmic domain of CD3 eta is 42 amino acids larger than that of CD3 zeta but lacks one of six potential tyrosine phosphorylation sites as well as a putative nucleotide binding site previously identified in CD3 zeta. These structural features presumably account for the difference between CD3 eta and CD3 zeta function and are consistent with the notion that CD3 eta may be an important component of a T-cell receptor isoform(s) during thymic development.

Full text

PDF
3319

Images in this article

3320Image
on p.3320
3323Image
on p.3323
3323Image
on p.3323

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baniyash M., Garcia-Morales P., Bonifacino J. S., Samelson L. E., Klausner R. D. Disulfide linkage of the zeta and eta chains of the T cell receptor. Possible identification of two structural classes of receptors. J Biol Chem. 1988 Jul 15;263(20):9874–9878. [PubMed] [Google Scholar]
  2. Baniyash M., Garcia-Morales P., Luong E., Samelson L. E., Klausner R. D. The T cell antigen receptor zeta chain is tyrosine phosphorylated upon activation. J Biol Chem. 1988 Dec 5;263(34):18225–18230. [PubMed] [Google Scholar]
  3. Baniyash M., Hsu V. W., Seldin M. F., Klausner R. D. The isolation and characterization of the murine T cell antigen receptor zeta chain gene. J Biol Chem. 1989 Aug 5;264(22):13252–13257. [PubMed] [Google Scholar]
  4. Clevers H., Alarcon B., Wileman T., Terhorst C. The T cell receptor/CD3 complex: a dynamic protein ensemble. Annu Rev Immunol. 1988;6:629–662. doi: 10.1146/annurev.iy.06.040188.003213. [DOI] [PubMed] [Google Scholar]
  5. Davis M. M., Bjorkman P. J. T-cell antigen receptor genes and T-cell recognition. Nature. 1988 Aug 4;334(6181):395–402. doi: 10.1038/334395a0. [DOI] [PubMed] [Google Scholar]
  6. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  7. Haskins K., Kubo R., White J., Pigeon M., Kappler J., Marrack P. The major histocompatibility complex-restricted antigen receptor on T cells. I. Isolation with a monoclonal antibody. J Exp Med. 1983 Apr 1;157(4):1149–1169. doi: 10.1084/jem.157.4.1149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hewick R. M., Hunkapiller M. W., Hood L. E., Dreyer W. J. A gas-liquid solid phase peptide and protein sequenator. J Biol Chem. 1981 Aug 10;256(15):7990–7997. [PubMed] [Google Scholar]
  9. Merćep M., Bonifacino J. S., Garcia-Morales P., Samelson L. E., Klausner R. D., Ashwell J. D. T cell CD3-zeta eta heterodimer expression and coupling to phosphoinositide hydrolysis. Science. 1988 Oct 28;242(4878):571–574. doi: 10.1126/science.2845582. [DOI] [PubMed] [Google Scholar]
  10. Merćep M., Weissman A. M., Frank S. J., Klausner R. D., Ashwell J. D. Activation-driven programmed cell death and T cell receptor zeta eta expression. Science. 1989 Dec 1;246(4934):1162–1165. doi: 10.1126/science.2531464. [DOI] [PubMed] [Google Scholar]
  11. Meuer S. C., Acuto O., Hercend T., Schlossman S. F., Reinherz E. L. The human T-cell receptor. Annu Rev Immunol. 1984;2:23–50. doi: 10.1146/annurev.iy.02.040184.000323. [DOI] [PubMed] [Google Scholar]
  12. Möller W., Amons R. Phosphate-binding sequences in nucleotide-binding proteins. FEBS Lett. 1985 Jul 1;186(1):1–7. doi: 10.1016/0014-5793(85)81326-0. [DOI] [PubMed] [Google Scholar]
  13. Orloff D. G., Frank S. J., Robey F. A., Weissman A. M., Klausner R. D. Biochemical characterization of the eta chain of the T-cell receptor. A unique subunit related to zeta. J Biol Chem. 1989 Sep 5;264(25):14812–14817. [PubMed] [Google Scholar]
  14. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sussman J. J., Bonifacino J. S., Lippincott-Schwartz J., Weissman A. M., Saito T., Klausner R. D., Ashwell J. D. Failure to synthesize the T cell CD3-zeta chain: structure and function of a partial T cell receptor complex. Cell. 1988 Jan 15;52(1):85–95. doi: 10.1016/0092-8674(88)90533-8. [DOI] [PubMed] [Google Scholar]
  16. Weissman A. M., Baniyash M., Hou D., Samelson L. E., Burgess W. H., Klausner R. D. Molecular cloning of the zeta chain of the T cell antigen receptor. Science. 1988 Feb 26;239(4843):1018–1021. doi: 10.1126/science.3278377. [DOI] [PubMed] [Google Scholar]
  17. Wierenga R. K., Hol W. G. Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant. Nature. 1983 Apr 28;302(5911):842–844. doi: 10.1038/302842a0. [DOI] [PubMed] [Google Scholar]
  18. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES