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Potassium channel tetramerization domain containing 1 (KCTD1) family members have a BTB/POZ domain, which can facilitate protein-protein interactions involved in the regulation of different signaling pathways. KCTD proteins have potential Zn 2+ /Cu 2+  binding sites with currently unknown structural and functional roles. We investigated potential Cu 2+ -specific effects on KCTD1 using circular dichroism, turbidity measurement, fluorescent dye binding, proteinase K (PK) digestion, cell proliferation and apoptosis assays. These experiments indicate that the KCTD1 secondary structure assumes greater β-sheet content and the proteins aggregate into a PK-resistant form under 20 μM Cu 2+ , and this β-sheet-rich aggregation with Cu 2+  promotes fibril formation, which results in increased cell toxicity by apoptosis. Our results reveal a novel role for Cu 2+  in determining the structure and function of KCTD1.

Bivalent Copper Ions Promote Fibrillar Aggregation of KCTD1 and Induce Cytotoxicity