Signal Integration by Translocation and Phosphorylation of PKCδ in the B Cell Alternate Pathway.

ABSTRACT: B cell signaling for activation via the BCR occurs as an isolated event only in vitro; in real life, BCR signaling takes place within a complex milieu that involves interactions with agents that trigger additional receptors. Chief among these is IL-4. We have shown that BCR signaling is reprogrammed by IL-4 receptor engagement and that this reprogramming involves creation of a new, signalosome-independent, Lyn-dependent alternate signaling pathway in B cells isolated from BALB/cByJ mice. A unique aspect of the alternate pathway is protein kinase Cδ (PKCδ) phosphorylation. In dissecting this pathway, we unexpectedly found that Lyn is associated with IL-4Rα, that IL-4 induces Lyn activation, and that Lyn immunoprecipitated from IL-4-treated B cells capably phosphorylates PKCδ in a cell-free

SUBMITTER: Khan N 

PROVIDER: S-EPMC8638162 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature