{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe provided abstract (1) does not mention VTRNA1-3. Instead, it focuses on the discovery and functional characterization of KCTD3 as an accessory subunit of native HCN3 channel complexes. KCTD3 binds specifically to the C-terminal region of HCN3, a binding that is essential for its regulatory role. The interaction of KCTD3 enhances cell surface expression and dramatically increases the current density of HCN3 channels, suggesting that it plays a significant role in modulating the channel’s biophysical properties and possibly neuronal excitability. Notably, while HCN3 can also interact with TRIP8b (another accessory protein), the study found no evidence for a complex containing both TRIP8b and KCTD3, indicating that KCTD3 acts in a distinct regulatory pathway."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xiaochun Cao-Ehlker, Xiangang Zong, Verena Hammelmann, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Up-regulation of hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3) by specific interaction with K+ channel tetramerization domain-containing protein 3 (KCTD3)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.434803"}], "href": "https://doi.org/10.1074/jbc.M112.434803"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23382386"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23382386"}]}]}]}