| First Author | Li J | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 37 | Pages | 28723-30 |
| PubMed ID | 20610380 | Mgi Jnum | J:166301 |
| Mgi Id | MGI:4844023 | Doi | 10.1074/jbc.M110.147868 |
| Citation | Li J, et al. (2010) Ankyrin-B regulates Kir6.2 membrane expression and function in heart. J Biol Chem 285(37):28723-30 |
| abstractText | Ankyrin polypeptides are critical for normal membrane protein expression in diverse cell types, including neurons, myocytes, epithelia, and erythrocytes. Ankyrin dysfunction results in defects in membrane expression of ankyrin-binding partners (including ion channels, transporters, and cell adhesion molecules), resulting in aberrant cellular function and disease. Here, we identify a new role for ankyrin-B in cardiac cell biology. We demonstrate that cardiac sarcolemmal K(ATP) channels directly associate with ankyrin-B in heart via the K(ATP) channel alpha-subunit Kir6.2. We demonstrate that primary myocytes lacking ankyrin-B display defects in Kir6.2 protein expression, membrane expression, and function. Moreover, we demonstrate a secondary role for ankyrin-B in regulating K(ATP) channel gating. Finally, we demonstrate that ankyrin-B forms a membrane complex with K(ATP) channels and the cardiac Na/K-ATPase, a second key membrane transporter involved in the cardiac ischemia response. Collectively, our new findings define a new role for cardiac ankyrin polypeptides in regulation of ion channel membrane expression in heart. |
