KCTD5 Forms Hetero-Oligomeric Complexes with Various Members of the KCTD Protein Family

Potassium Channel Tetramerization Domain 5 (KCTD5) regulates diverse aspects of physiology, ranging from neuronal signaling to colorectal cancer. A key feature of KCTD5 is its self-assembly into multi-subunit oligomers that seemingly enables participation in an array of protein-protein interactions....

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Published inInternational journal of molecular sciences Vol. 24; no. 18; p. 14317
Main Authors Liao, Yini, Sloan, Douglas C, Widjaja, Josephine H, Muntean, Brian S
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 01.09.2023
MDPI
Subjects
Antibodies
Colorectal cancer
Disease
Ethylenediaminetetraacetic acid
Experiments
KCTD12
KCTD17
KCTD2
KCTD5
KCTD8
Oligomers
Potassium Channel Tetramerization Domain (KCTD)-containing protein
Potassium Channels - genetics
Potassium Channels - metabolism
Proteins
Signal Transduction
KCTD8
Potassium Channel Tetramerization Domain (KCTD)-containing protein
hetero-oligomer
KCTD2
KCTD12
KCTD17
KCTD5
KCTD16
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Summary:Potassium Channel Tetramerization Domain 5 (KCTD5) regulates diverse aspects of physiology, ranging from neuronal signaling to colorectal cancer. A key feature of KCTD5 is its self-assembly into multi-subunit oligomers that seemingly enables participation in an array of protein-protein interactions. KCTD5 has recently been reported to form hetero-oligomeric complexes with two similar KCTDs (KCTD2 and KCTD17). However, it is not known if KCTD5 forms hetero-oligomeric complexes with the remaining KCTD protein family which contains over two dozen members. Here, we demonstrate that KCTD5 interacts with various KCTD proteins when assayed through co-immunoprecipitation in lysed cells. We reinforced this dataset by examining KCTD5 interactions in a live-cell bioluminescence resonance energy transfer (BRET)-based approach. Finally, we developed an IP-luminescence approach to map regions on KCTD5 required for interaction with a selection of KCTD that have established roles in neuronal signaling. We report that different regions on KCTD5 are responsible for uniquely contributing to interactions with other KCTD proteins. While our results help unravel additional interaction partners for KCTD5, they also reveal additional complexities in KCTDs' biology. Moreover, our findings also suggest that KCTD hetero-oligomeric interactions may occur throughout the KCTD family.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms241814317