Role of Two Conserved Cytoplasmic Threonine Residues (T410 and T412) in CD5 Signaling

CD5 is a transmembrane coreceptor that modulates activation and differentiation signals mediated by the Ag-specific receptor present on both T and B1a lymphocytes. CD5 lacks intrinsic catalytic activity, and its immunomodulatory properties result from intracellular interactions mediated by the CD5 c...

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Bibliographic Details
Published in:The Journal of immunology (1950) 2001-01, Vol.166 (1), p.396-402
Main Authors: Vila, Josep M, Calvo, Javier, Places, Lourdes, Padilla, Olga, Arman, Monica, Gimferrer, Idoia, Aussel, Claude, Vives, Jordi, Lozano, Francisco
Format: Article
Language:English
Subjects:
Amino Acid Substitution - genetics
Amino Acid Substitution - immunology
Animals
Antibodies, Monoclonal - pharmacology
CD5 antigen
CD5 Antigens - genetics
CD5 Antigens - immunology
CD5 Antigens - metabolism
CD5 Antigens - physiology
Cell Membrane - immunology
Cell Membrane - metabolism
Conserved Sequence
Cytoplasm - genetics
Cytoplasm - immunology
Diglycerides - metabolism
Humans
Jurkat Cells
Peptide Fragments - immunology
Peptide Fragments - metabolism
Phosphorylation - drug effects
Protein Kinase C - physiology
Rats
Signal Transduction - drug effects
Signal Transduction - genetics
Signal Transduction - immunology
Tetradecanoylphorbol Acetate - pharmacology
Threonine - genetics
Threonine - metabolism
Threonine - physiology
Transfection
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Summary:CD5 is a transmembrane coreceptor that modulates activation and differentiation signals mediated by the Ag-specific receptor present on both T and B1a lymphocytes. CD5 lacks intrinsic catalytic activity, and its immunomodulatory properties result from intracellular interactions mediated by the CD5 cytoplasmic tail. The nature of these interactions is currently a matter of investigation. Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. Functional studies revealed that the integrity of T410 and T412 is also critical for CD5-mediated phosphatidylcholine-specific phospholipase C (PC-PLC) activation and phorbol ester-mediated inhibition of Ab-induced internalization of CD5. These results strongly argue in favor of a role for T410 and T412 in the signaling mediated by CD5.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.166.1.396