Research ExplorerPublicationsThe BTB domains of the potassium channel tetramerization dom...

The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states

Standard

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, Vol. 590, No. 11, 06.2016, p. 1663-71.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Smaldone, G, Pirone, L, Pedone, E, Marlovits, T, Vitagliano, L & Ciccarelli, L 2016, 'The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states', FEBS LETT, vol. 590, no. 11, pp. 1663-71. https://doi.org/10.1002/1873-3468.12203

APA

Smaldone, G., Pirone, L., Pedone, E., Marlovits, T., Vitagliano, L., & Ciccarelli, L. (2016). The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states. FEBS LETT, 590(11), 1663-71. https://doi.org/10.1002/1873-3468.12203

Vancouver

Smaldone G, Pirone L, Pedone E, Marlovits T, Vitagliano L, Ciccarelli L. The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states. FEBS LETT. 2016 Jun;590(11):1663-71. https://doi.org/10.1002/1873-3468.12203

Bibtex

@article{3b1f88c5bf6f4886a16023eafb3ba0d9,
title = "The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states",
abstract = "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-{\`a}-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.",
keywords = "Letter",
author = "Giovanni Smaldone and Luciano Pirone and Emilia Pedone and Thomas Marlovits and Luigi Vitagliano and Luciano Ciccarelli",
note = "{\textcopyright} 2016 Federation of European Biochemical Societies.",
year = "2016",
month = jun,
doi = "10.1002/1873-3468.12203",
language = "English",
volume = "590",
pages = "1663--71",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "11",

}

RIS

TY - JOUR

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 -