Members of the KCTD (Potassium Channel Tetramerization Domain) family represent an emerging class of proteins that play a key role in fundamental physio-pathological processes. The unifying trait of KCTD proteins is the presence of a BTB(Bric-a-brac, Tramtrack, Broad complex) domain in their N-terminal region. On the other hand, their C-terminal region presents a remarkable variability. Investigations carried out in the last decade have highlighted analogies and differences among different members from both the structural and the functional points of view. Although the biochemical activities of these proteins are still somehow obscure, the biological characterizations of KCTDs have disclosed their crucial roles in highly diversified processes such as protein ubiquitination and degradation, binding and modulation of the GABAB receptor, autophagy, adipogenesis, sleep homeostasis and metabolic homeostasis. Not surprisingly, they are also involved in the insurgence of severe pathological states that include epilepsy, cancer, obesity, and skin diseases. A number of these pathologies are generated by mutations of KCTD proteins whose structural interpretations have been scarcely investigated. Considering the fundamental role played by this protein family, our research interest is focused on the structural and functional characterization of different members in order to develop molecules able to modulate the function of the protein. To reach this aim, DNA recombinant techniques together with biochemical and biophysical methodologies are used.
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