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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