Fig. 11.

Catalytic activities of CK1ε and CK1α are increased in polycystic kidneys. CK1ε (A) and CK1α (B) were immunopurified with specific antibodies from kidneys of jck, Pkd1-cKO, Thm1-cKO, and Nphp4 mutant mice and their control WT littermates. Catalytic activities were assayed using ³³P-ATP and a peptide substrate. Activities are reported as ³³P-phosphate incorporated/30 min incubation. Number of different assays (CK1ε/CK1α): 2/2 (Jck), 5/3 (Pkd1cKO), 2/2 (Thm1cKO), and 3/3 (Nphp4). Tested in triplicate. CK1ε (C) and CK1α (D) were immunopurified with specific antibodies from kidneys, liver, heart, and brain of Pkd1-cKO and control mice. Their catalytic activities were assayed with ³³P-ATP and a peptide substrate. Activities are reported as ³³P-phosphate incorporated/30 min incubation. Numbers inside parentheses represent the kinase activity fold change in recombinant vs. wild-type and control tissues. Number of different assays (CK1ε/CK1α): 5/3 (kidneys), 3/3 (liver), 3/3 (brain), and 3/3 (heart).