| First Author | Kim H | Year | 2018 |
| Journal | Cell Calcium | Volume | 71 |
| Pages | 75-85 | PubMed ID | 29604966 |
| Mgi Jnum | J:352397 | Mgi Id | MGI:6859883 |
| Doi | 10.1016/j.ceca.2017.12.003 | Citation | Kim H, et al. (2018) Anoctamin 9/TMEM16J is a cation channel activated by cAMP/PKA signal. Cell Calcium 71:75-85 |
| abstractText | Anoctamins (ANOs) are multifunctional membrane proteins that consist of 10 homologs. ANO1 (TMEM16A) and ANO2 (TMEM16B) are anion channels activated by intracellular calcium that meditate numerous physiological functions. ANO6 is a scramblase that redistributes phospholipids across the cell membrane. The other homologs are not well characterized. We found ANO9/TMEM16J is a cation channel activated by a cAMP-dependent protein kinase A (PKA). Intracellular cAMP-activated robust currents in whole cells expressing ANO9, which were inhibited by a PKA blocker. A cholera toxin that persistently stimulated adenylate cyclase activated ANO9 as did the application of PKA. The cAMP-induced ANO9 currents were permeable to cations. The cAMP-dependent ANO9 currents were augmented by intracellular Ca(2+). Ano9 transcripts were predominant in the intestines. Human intestinal SW480 cells expressed high levels of Ano9 transcripts and showed PKA inhibitor-reversible cAMP-dependent currents. We conclude that ANO9 is a cation channel activated by a cAMP/PKA pathway and could play a role in intestine function. |
