Sp. Sidorenko et al., PROTEIN-KINASE-C-MU (PKC-MU) ASSOCIATES WITH THE B-CELL ANTIGEN RECEPTOR COMPLEX AND REGULATES LYMPHOCYTE SIGNALING, Immunity, 5(4), 1996, pp. 353-363
We have identified a Ser/Thr kinase associated with the B cell recepto
r (BCR) complex as protein kinase C mu (PKC mu). PKC mu activity is up
-regulated after crosslinking the BCR and CD19 on B cells, and PKC mu
coprecipitates with Syk and phospholipase C-gamma 1/2 (PLC gamma 1/2).
In vitro phosphorylation of fusion proteins showed that both Syk and
PLC gamma 1 are potential substrates of PKC mu in vivo. Analysis of mu
tants of the chicken B cell line DT40 deficient in either Syk, Lyn, Bt
k, or PLC gamma 2 revealed that BCR-induced activation of PKC mu, like
activation of PLC gamma 2, requires Syk and is partially regulated by
Btk, but is Lyn independent. PKC mu can down-regulate the ability of
Syk to phosphorylate PLC gamma 1 in vitro. Thus, PKC mu may function i
n a negative feedback loop regulating BCR-initiated signaling cascades
.