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The RIG-I-like receptors (RLRs) signal innate immune defenses upon RNA virus infection, but their roles in adaptive immunity have not been clearly defined. Here, we showed that the RLR LGP2 was not essential for induction of innate immune defenses, but rather was required for controlling antigen-specific CD8 + T cell survival and fitness during peripheral T cell-number expansion in response...
Recent studies have demonstrated that the skin of a normal adult human contains 10–20 billion resident memory T cells, including various helper, cytotoxic, and regulatory T cell subsets, that are poised to respond to environmental antigens. Using only autologous human tissues, we report that both in vitro and in vivo, resting epidermal Langerhan cells (LCs) selectively and specifically induced the...
Adaptor proteins act as conduits to channel upstream signals into downstream effector branches. Two B cell-associated adaptors, Bam32 and Carma1, regulate the ERK, JNK, and NF-κB branches of the BCR signaling pathway. Recent studies of Bam32 -/- and Carma1 -/- mice suggest that each adaptor controls a distinct conduit regulating either only proliferation (Bam32)...
In this issue of Immunity, Brodeur et al. show that C4b binding protein (C4BP), a regulator component of the classical complement (C) pathway, can bind to CD40 receptors on B cells and activate them. This suggests a novel way by which CD40 may function to bridge innate and adaptive immune responses.
A B lymphocyte hyperactivity syndrome resembling systemic lupus erythematosus characterizes mice lacking the src-family kinase Lyn. Lyn is not required to initiate B cell antigen receptor (BCR) signaling but is an essential inhibitory component. lyn −/− B cells have a delayed but increased calcium flux and exaggerated negative selection responses in the presence of antigen and spontaneous...
We have identified a Ser/Thr kinase associated with the B cell receptor (BCR) complex as protein kinase C μ (PKCμ). PKCμ activity is up-regulated after crosslinking the BCR and CD19 on B cells, and PKCμ coprecipitates with Syk and phospholipase C-μ1/2 (PLCγ1/2). In vitro phosphorylation of fusion proteins showed that both Syk and PLCγ1 are potential substrates of PKCμ in vivo. Analysis of mutants...
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