Receptor signalling events including those initiated following activation of cytokine and growth factor receptors and the well-characterised death receptors (tumour necrosis factor receptor, type 1, FasR and TRAIL-R1/2) are initiated at the cell surface through the recruitment and formation of intracellular multiprotein signalling complexes that activate divergent signalling pathways. Over the past decade, research studies reveal that many of these receptor-initiated signalling events involve the sequential proteolysis of specific receptors by membrane-bound proteases and the γ-secretase protease complexes. Proteolysis enables the liberation of soluble receptor ectodomains and the generation of intracellular receptor cytoplasmic domain fragments. The combined and sequential enzymatic activity has been defined as regulated intramembrane proteolysis and is now a fundamental signal transduction process involved in the termination or propagation of receptor signalling events. In this review, we discuss emerging evidence for a role of the γ-secretase protease complexes and regulated intramembrane proteolysis in cell- and immune-signalling pathways.
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Cover Image
Cover Image
Cryo-electron microscopy density map of a Cowpea Mosaic virus (CPMV) empty virus-like particle (eVLP) at 2.7 Å resolution (EMD-3952). The large (L) subunit is displayed in green and the small (S) subunit in blue. Five S subunits interact to form pronounced turrets at the 5-fold axis. Here we show a view down a two-fold axis. The eVLP was produced by transient co-expression in plants of the precursor of the L and S subunits (VP60) and the virus-encoded protease (24K) required for its processing. For further details, please see article by Lomonossoff et al, pages 1263–1269
Regulated intramembrane proteolysis: emergent role in cell signalling pathways
Aonghus J. McCarthy, Caroline Coleman-Vaughan, Justin V. McCarthy; Regulated intramembrane proteolysis: emergent role in cell signalling pathways. Biochem Soc Trans 15 December 2017; 45 (6): 1185–1202. doi: https://doi.org/10.1042/BST20170002
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