دورية أكاديمية
KCTD5 Forms Hetero-Oligomeric Complexes with Various Members of the KCTD Protein Family.
| العنوان: | KCTD5 Forms Hetero-Oligomeric Complexes with Various Members of the KCTD Protein Family. |
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| المؤلفون: | Liao, Yini, Sloan, Douglas C., Widjaja, Josephine H., Muntean, Brian S. |
| المصدر: | International Journal of Molecular Sciences; Sep2023, Vol. 24 Issue 18, p14317, 14p |
| مصطلحات موضوعية: | POTASSIUM channels, FLUORESCENCE resonance energy transfer, PROTEIN-protein interactions, PROTEINS |
| مستخلص: | 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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: | Complementary Index |
Full Text Finder | تدمد: | 16616596 |
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| DOI: | 10.3390/ijms241814317 |