| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10759960 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
⺠Caveolin-3 (cav3) directly interacts with large conductance Ca2+ activated K+ (BKCa) channel. ⺠Single molecular images were obtained by total internal reflection fluorescent (TIRF) microscopy. ⺠Direct molecular interaction was detected as fluorescent resonance energy transfer (FRET). ⺠Cav3 binds to a specific C terminus domain of BKCa channel. ⺠The interaction with cav3 regulates BKCa channel trafficking to cell surface and their accumulation to caveola.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Yoshiaki Suzuki, Hisao Yamamura, Susumu Ohya, Yuji Imaizumi,