The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states
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The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states. / Smaldone, Giovanni; Pirone, Luciano; Pedone, Emilia; Marlovits, Thomas; Vitagliano, Luigi; Ciccarelli, Luciano.
in: FEBS LETT, Jahrgang 590, Nr. 11, 06.2016, S. 1663-71.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states
AU - Smaldone, Giovanni
AU - Pirone, Luciano
AU - Pedone, Emilia
AU - Marlovits, Thomas
AU - Vitagliano, Luigi
AU - Ciccarelli, Luciano
N1 - © 2016 Federation of European Biochemical Societies.
PY - 2016/6
Y1 - 2016/6
N2 - 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(BTB) in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.
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(BTB) in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.
KW - Letter
U2 - 10.1002/1873-3468.12203
DO - 10.1002/1873-3468.12203
M3 - SCORING: Journal article
C2 - 27152988
VL - 590
SP - 1663
EP - 1671
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 11
ER -