The BTB-Containing Protein Kctd15 Is SUMOylated In Vivo
- Authors
- Zarelli, V.E., and Dawid, I.B.
- ID
- ZDB-PUB-131105-14
- Date
- 2013
- Source
- PLoS One 8(9): e75016 (Journal)
- Registered Authors
- Dawid, Igor B., Zarelli, Valeria
- Keywords
- none
- MeSH Terms
-
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- HEK293 Cells
- Humans
- Molecular Sequence Data
- Mutant Proteins/metabolism
- Neural Crest/metabolism
- Potassium Channels/chemistry
- Potassium Channels/metabolism*
- Potassium Channels, Voltage-Gated/chemistry
- Potassium Channels, Voltage-Gated/metabolism*
- Protein Binding
- Protein Transport
- Recombinant Fusion Proteins/metabolism
- SUMO-1 Protein/metabolism
- Subcellular Fractions/metabolism
- Substrate Specificity
- Sumoylation*
- Transcription Factor AP-2/metabolism
- Zebrafish/metabolism
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/metabolism*
- PubMed
- 24086424 Full text @ PLoS One
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, ωKxE, 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.