Animal cells and systems

The Korean Society for Integrative Biology (한국통합생물학회)
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Chimeric Protein of CD8a Extracellular Domain and CD4 Transmembrane and Cytoplasmic Domain Binds More Efficiently to p561ck than CD8a

  • Young Il Choi (Institute of Molecular Biology and Genetics and Department of Molecular Biology, Seoul National University) ;
  • Sang Dai Park (Institute of Molecular Biology and Genetics and Department of Molecular Biology, Seoul National University) ;
  • Rho Hyun Seong (Institute of Molecular Biology and Genetics and Department of Molecular Biology, Seoul National University)
  • Published : 1999.09.01
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Abstract

p56$^{Ick}$, a cytoplasmic protein tyrosine kinase of the src family, is non-covalently associated with the cell surface coreceptors CD4 and CD8, which are expressed on thymocytes and mature T cells. The coreceptor protein plays an important role during the differentiation of thymocytes and the activation of T cells. DNA constructs were designed to study the roles of CD4 and CD8 during the differentiation of thymocytes. One is a chimeric cDNA which consists of coding regions for the extracellular domain of CD8a and the transmembrane and cytoplasmic domain of CD4. The other is the same chimeric cDNA but with a point mutation converting Cys to Ala in the Ick-binding site to disrupt the association. We confirmed that the CD8a/CD4 chimeric molecule bound to Ick more efficiently than the wild type CD8a protein. However, the chimeric protein with the Cys$leftrightarro$Ala mutation did not associate with Ick. The results suggest a possibility that the CD8a/CD4 chimeric protein may behave like a CD4 protein in associating with Ick and that it may deliver a signal inside the cell in a similar manner, Analysing effects of the mutant CD8a/CD4 chimeric protein expression in developing thymocytes will elucidate the role of Ick during the determination of CD4/CD8 cell lineages.

Keywords

References

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