Toll‐like receptors stimulate regulated intramembrane proteolysis of the CSF‐1 receptor through Erk activation

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Abstract
The CSF‐1 receptor is a protein‐tyrosine kinase that regulates the renewal, differentiation and activation of monocytes and macrophages. We have recently shown that the CSF‐1 receptor undergoes regulated intramembrane proteolysis, or RIPping. Here, we report that RIPping can be observed in response to pathogen‐associated molecules, which act through Toll‐like receptors (TLRs). TLR‐induced CSF‐1 receptor RIPping is largely independent of protein kinase C, while maximal RIPping depends on Erk activation. Our studies show that CSF‐1 receptor RIPping can be activated by various intracellular signal transduction pathways and that RIPping is likely to play an important role during macrophage activation.