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, Mitogen-Activated Protein Kinase Kinase, and c-Jun NH2-Terminal Kinase1
*
Servei d’Immunologia, Institut D’Investigacions Biomèdiques August Pi i Sunyer, Hospital Clínic, Barcelona, Spain; and
Division of Biology, California Institute of Technology, Pasadena, CA 91125
The CD5 lymphocyte surface glycoprotein is a coreceptor involved in
the modulation of Ag-specific receptor-mediated activation and
differentiation signals. The molecular basis for its modulatory
properties is not yet well understood. In the present study we describe
early biochemical events triggered by CD5 stimulation, which include
the phosphatidylcholine-specific phospholipase C (PC-PLC)-dependent
activation of acidic sphingomyelinase (A-SMase) in normal and
lymphoblastoid T and B cells. The functional coupling of PC-PLC and
A-SMase is demonstrated by the abrogation of A-SMase activation by 1)
xanthogenate tricyclodecan-9-yl (D609), a selective inhibitor of
PC-PLC, and 2) replacement of several C-terminal serine residues (S458,
S459, and S461) present in the cytoplasmic tail of CD5 that are known
to be critical for PC-PLC activation. Additionally, we demonstrate that
activation of protein kinase C-
(PKC-) and members of the
mitogen-activated protein kinase (MAPK) cascade (MAPK kinase and c-Jun
NH2-terminal kinase), but not the NF-
B, are downstream
events of the CD5 signaling pathway. A-SMase, PKC-, and MAPK family
members are key mediators of cell responses as diverse as
proliferation, differentiation, and growth arrest and may contribute to
CD5-mediated modulation of TCR or BCR signaling.
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