PMC:1942070 / 8937-13150 JSONTXT

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Hence, BCR-induced activation of the Akt, mTOR/p70 S6 kinase (as shown by S6 ribosomal protein phosphorylation) and MAPK signalling pathways was clearly detectable in PKD1/3-null B cells (Fig. 3B). Furthermore, enhanced tyrosine phosphorylation of multiple cellular proteins as well as an increase in intracellular calcium levels was also observed following BCR stimulation of PKD1/3-null B cells (data not shown). We did observe that the strength of BCR (but not phorbol ester)-induced regulation of the Erk1-RSK1 signalling pathway was reduced in PKD1/3−/− B cells compared to wild-type B cells (Fig. 3B). One interpretation of this data is that PKD enzymes may modulate Erk activation. Indeed, PKD enzymes have previously been linked to the growth factor-regulated Erk signalling in fibroblast and endothelial cell lines [33–35]. However, BCR-induced Erk phosphorylation was also reduced in PKD1/3−/−-Flag-PKD3+ B cells (data not shown) suggesting that reduced BCR levels on the surface of PKD1/3−/− (and PKD1/3−/−-Flag-PKD3+) B cells may itself impact on the strength of activation of this specific intracellular signalling pathway.\nTo search for other potential PKD targets that may show defective regulation in PKD1/3−/− DT40 B cells, we used a PKD substrate phospho-antibody that recognises consensus phosphorylation sequences targeted by PKD enzymes (LxRxxpS/T) [36]. As shown in Fig. 3C, phorbol ester- and BCR-induced phosphorylation of cellular substrates detected by this phospho-antibody was similar in wild-type and PKD1/3−/− cells and is therefore independent of PKD enzymes. However, pretreatment of both wild-type and PKD1/3−/− DT40 B cells with GF109203X, a bisindoylmaleimide derivative that inhibits PKCs prevented the induction of proteins that contain phosphorylated LxRxxS/T motifs. Thus loss of PKD1/3 enzymes does not globally disrupt the phosphorylation of cellular proteins that contain LxRxxpS/T motifs. This result is perhaps not surprising as LxRxxS/T motifs also act as good substrates for other serine/threonine kinases such as MAPKAPK2. However these experiments do provide further evidence that phosphospecific antisera are not sufficiently selective to be designated kinase specific substrate antisera.\nBCR-induced signalling pathways culminate in the activation of gene transcription events that control B cell survival, proliferation and function. In this context, it has been proposed that PKD family members control of gene transcription through activation of the NFκB transcription factor. Thus, PKD-mediated activation of NFκB occurs downstream of a variety of different signals, including mROS/oxidative stress, lysophosphatidic acid and the Bcr-Abl oncogene [17,21,23,30,37]. Furthermore, expression of an activated PKD1 mutant enhances HPK1-mediated NFκB activation [38]. In B cells, NFκB is known to be regulated via DAG and PKCβ [39,40] but whether PKDs are key intermediaries for NFκB regulation has not been explored.\nThe data (Fig. 4A) show that NFκB transcriptional activity was strongly induced in both wild-type and PKD1/3−/− DT40 B cells in response to either phorbol ester or BCR stimulation. In contrast, BCR and phorbol ester-induced NFκB transcriptional activity was abolished in PKCβ−/− DT40 B cells (Fig. 4A), although strong activation of PKD kinases (as assessed by autophosphorylation of PKD1 at S916) was observed in the PKCβ−/− cells (Fig. 4B). Thus, PKD kinases are neither essential nor sufficient to mediate BCR-induced NFκB activation in DT40 B cells and hence do not participate in DAG/PKC mediated control of 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