TY - JOUR

T1 - Distinct domains of the CD3-gamma chain are involved in surface expression and function of the T cell antigen receptor

AU - Wegener, A M

AU - Hou, X

AU - Dietrich, J

AU - Geisler, C

N1 - Keywords: Antigens, CD3; Cell Line; Down-Regulation; Humans; Phosphotyrosine; Protein Kinase C; Protein Processing, Post-Translational; Receptors, Antigen, T-Cell; Recombinant Fusion Proteins; Transfection; Tyrosine

PY - 1995

Y1 - 1995

N2 - The T cell antigen receptor (TcR) is a multisubunit complex that consists of at least six different polypeptides. We have recently demonstrated that the CD3-delta subunit cannot substitute for the CD3-gamma subunit in TcR cell surface expression, in spite of significant amino acid homology between these two subunits. To identify CD3-gamma-specific domains that are required for assembly of the complete TcR and for surface expression and function of the TcR, chimeric CD3-gamma/CD3-delta molecules were constructed and expressed in T cells devoid of endogenous CD3-gamma. Substitution of the extracellular domain of CD3-gamma with that of CD3-delta did not allow cell surface expression of the TcR. In contrast, substitution of the transmembrane and/or the intracellular domains of CD3-gamma with those of CD3-delta did allow TcR cell surface expression. These results conclusively demonstrate that the extracellular domain of CD3-gamma plays a unique role in TcR assembly. Functional analyses of the transfectants demonstrated that the intracellular domain of CD3-gamma is required for protein kinase C-mediated down-regulation of TcR but is dispensable for the pattern of tyrosine phosphorylation observed following activation through TcR.

AB - The T cell antigen receptor (TcR) is a multisubunit complex that consists of at least six different polypeptides. We have recently demonstrated that the CD3-delta subunit cannot substitute for the CD3-gamma subunit in TcR cell surface expression, in spite of significant amino acid homology between these two subunits. To identify CD3-gamma-specific domains that are required for assembly of the complete TcR and for surface expression and function of the TcR, chimeric CD3-gamma/CD3-delta molecules were constructed and expressed in T cells devoid of endogenous CD3-gamma. Substitution of the extracellular domain of CD3-gamma with that of CD3-delta did not allow cell surface expression of the TcR. In contrast, substitution of the transmembrane and/or the intracellular domains of CD3-gamma with those of CD3-delta did allow TcR cell surface expression. These results conclusively demonstrate that the extracellular domain of CD3-gamma plays a unique role in TcR assembly. Functional analyses of the transfectants demonstrated that the intracellular domain of CD3-gamma is required for protein kinase C-mediated down-regulation of TcR but is dispensable for the pattern of tyrosine phosphorylation observed following activation through TcR.

M3 - Journal article

C2 - 7533164

VL - 270

SP - 4675

EP - 4680

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -