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(Received for publication, October 23, 1995)
The B cell antigen receptor complex contains heterodimers of
Ig-
and Ig-
. The cytoplasmic tails of each of these chains
contain two conserved tyrosines, phosphorylation of which initiates the
signal transduction cascades activated by the receptor complex.
Although the cytoplasmic domains of Ig- and Ig- have been
expressed individually and demonstrated to be competent signal
transduction units, we postulated that within the context of a
heterodimer, Ig- and Ig- could have new, complementary or
even synergistic functions. Therefore we developed a system to compare
the signal transducing capacities of dimers of Ig-/Ig-,
Ig-/Ig-, or Ig-/Ig-. This was done by fusing the
extracellular and transmembrane domains of either human
platelet-derived growth factor receptor (PDGFR) or to the
cytoplasmic tail of either Ig- or Ig-. Three cell lines
expressing PDGFR/Ig-, PDGFR/Ig-, or
PDGFR/Ig- together with PDGFR/Ig- were established
in the murine B cell line A20 IIA1.6. While aggregation of each dimer
by itself could induce the tyrosine phosphorylation of cellular
substrates, only aggregation of the heterodimer induced the
phosphorylation of substrates similar in range and intensity to that
induced by the endogenous B cell antigen receptor complex.
Interestingly, Ig- remarkably enhanced the rapidity (T
decreased from 5 to 1 min) and intensity
(greater than 10-fold enhancement) of Ig- phosphorylation.
Conversely, the phosphorylation of Ig- was reduced to undetectable
levels when co-aggregated with Ig-. The enhancement of Ig-
phosphorylation by Ig- correlated with a lowering of the
stimulation threshold for tyrosine kinase activation.
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