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

Authors
Kim, HyunhoKang, Ah-YoungKo, Ah-raPark, Hayne ChoSo, InsukPark, Jong HoonCheong, Hae IlHwang, Young-HwanAhn, Curie
Issue Date
Jan-2014
Publisher
ELSEVIER INC
Keywords
Polycystic kidney disease; Polycystin-1; Calpain; PEST; Calcium homeostasis
Citation
EXPERIMENTAL CELL RESEARCH, v.320, no.1, pp 62 - 68
Pages
7
Journal Title
EXPERIMENTAL CELL RESEARCH
Volume
320
Number
1
Start Page
62
End Page
68
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11020
DOI
10.1016/j.yexcr.2013.10.012
ISSN
0014-4827
1090-2422
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 mu- 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. (C) 2013 The Authors. Published by Elsevier Inc. All rights reserved.
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