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. 2014 Aug 4;9(8):e103994. doi: 10.1371/journal.pone.0103994

Figure 7. Diagram to elucidate a possible mechanism of how fluoride activates the Gαq signaling pathway, in turn stabilizing SATB1 protein in secretory ameloblasts.

Figure 7

This possible mechanism suggests that fluoride can combine with other ions (X) to mimic the chemical structure of γ-phosphate. Upon entering the cells, ion/fluoride complex (XFn) (such as AlF4) can bind to GDP, together to activate Gαq protein in ameloblasts, which in turn activates phospholipase C β (PLCβ) that cleaves phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Increased DAG sequentially activates PKC, which can then phosphorylate SATB1. SATB1 can be hydrolyzed by caspase-6, while phosphorylation prevents SATB1 from hydrolyzing by caspase-6, resulting in an apparent relative increase in SATB1 in cells.