Distinct domains of the CD3-gamma chain are involved in surface expression and function of the T cell antigen receptor
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Distinct domains of the CD3-gamma chain are involved in surface expression and function of the T cell antigen receptor. / Wegener, A M; Hou, X; Dietrich, J; Geisler, C.
In: Journal of Biological Chemistry, Vol. 270, No. 9, 1995, p. 4675-80.Research output: Contribution to journal › Journal article › Research › peer-review
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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 -
ID: 8545862