TY  - JOUR
AU  - Smaldone, Giovanni
AU  - Pirone, Luciano
AU  - Pedone, Emilia
AU  - Marlovits, Thomas
AU  - Vitagliano, Luigi
AU  - Ciccarelli, Luciano
TI  - The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states
JO  - FEBS letters
VL  - 590
IS  - 11
SN  - 0014-5793
CY  - Chichester
PB  - Wiley
M1  - PUBDB-2017-00420
SP  - 1663 - 1671
PY  - 2016
N1  - © Federation of European Biochemical Societies ; Post referee fulltext in progress; Embargo 12 months from publication
AB  - Potassium channel tetramerization domain-containing (KCTD) proteins are involved in fundamental physio-pathological processes. Here, we report an analysis of the oligomeric state of the Bric-à-brack, Tram-track, Broad complex (BTB) domains of seven distinct KCTDs belonging to five major clades of the family evolution tree. Despite their functional and sequence variability, present electron microscopy data highlight the occurrence of well-defined pentameric states for all domains. Our data also show that these states coexist with alternative forms which include open pentamers. Thermal denaturation analyses conducted using KCTD1 as a model suggest that, in these proteins, different domains cooperate to their overall stability. Finally, negative-stain electron micrographs of KCTD6<sup>BTB</sup> in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000377795000011
C6  - pmid:27152988
DO  - DOI:10.1002/1873-3468.12203
UR  - https://bib-pubdb1.desy.de/record/317079
ER  -