The BTB-containing protein Kctd15 is SUMOylated in vivo.
PLoS One
; 8(9): e75016, 2013.
Article
em En
| MEDLINE
| ID: mdl-24086424
ABSTRACT
Potassium Channel Tetramerization Domain containing 15 (Kctd15) has a role in regulating the neural crest (NC) domain in the embryo. Kctd15 inhibits NC induction by antagonizing Wnt signaling and by interaction with the transcription factor AP-2α activation domain blocking its activity. Here we demonstrate that Kctd15 is SUMOylated by SUMO1 and SUMO2/3. Kctd15 contains a classical SUMO interacting motif, ψKxE, at the C-terminal end, and variants of the motif within the molecule. Kctd15 SUMOylation occurs exclusively in the C-terminal motif. Inability to be SUMOylated did not affect Kctd15's subcellular localization, or its ability to repress AP-2 transcriptional activity and to inhibit NC formation in zebrafish embryos. In contrast, a fusion of Kctd15 and SUMO had little effectiveness in AP-2 inhibition and in blocking of NC formation. These data suggest that the non-SUMOylated form of Kctd15 functions in NC development.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Canais de Potássio
/
Canais de Potássio de Abertura Dependente da Tensão da Membrana
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Proteínas de Peixe-Zebra
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Sumoilação
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article