Calpain-mediated proteolysis of polycystin-1 C-terminus induces JAK2 and ERK signal alterations

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Abstract

Autosomal dominant polycystic kidney disease (ADPKD), a hereditary renal disease caused by mutations in PKD1 (85%) or PKD2 (15%), is characterized by the development of gradually enlarging multiple renal cysts and progressive renal failure. Polycystin-1 (PC1), PKD1 gene product, is an integral membrane glycoprotein which regulates a number of different biological processes including cell proliferation, apoptosis, cell polarity, and tubulogenesis. PC1 is a target of various proteolytic cleavages and proteosomal degradations, but its role in intracellular signaling pathways remains poorly understood. Herein, we demonstrated that PC1 is a novel substrate for μ- and m-calpains, which are calcium-dependent cysteine proteases. Overexpression of PC1 altered both Janus-activated kinase 2 (JAK2) and extracellular signal-regulated kinase (ERK) signals, which were independently regulated by calpain-mediated PC1 degradation. They suggest that the PC1 function on JAK2 and ERK signaling pathways might be regulated by calpains in response to the changes in intracellular calcium concentration. © 2013 The Authors.

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Kim, H., Kang, A. Y., Ko, A. ra, Park, H. C., So, I., Park, J. H., … Ahn, C. (2014). Calpain-mediated proteolysis of polycystin-1 C-terminus induces JAK2 and ERK signal alterations. Experimental Cell Research, 320(1), 62–68. https://doi.org/10.1016/j.yexcr.2013.10.012

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