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

作者：Glenn Gary; van der Geer Peter^*

来源：FEBS LETTERS, 2008, 582(6): 911-915.

DOI：10.1016/j.febslet.2008.02.029

• signal transduction
• protein-tyrosine kinase
• RIPping
• TACE
• PKC

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.

• 出版日期2008-3-19