| First Author | Qu Z | Year | 2006 |
| Journal | FEBS Lett | Volume | 580 |
| Issue | 8 | Pages | 2141-6 |
| PubMed ID | 16563389 | Mgi Jnum | J:107638 |
| Mgi Id | MGI:3621587 | Doi | 10.1016/j.febslet.2006.03.025 |
| Citation | Qu Z, et al. (2006) A short motif in the C-terminus of mouse bestrophin 4 inhibits its activation as a Cl channel. FEBS Lett 580(8):2141-6 |
| abstractText | Bestrophins are a new family of anion channels. Here, we examined the Cl channel activity of mBest4. Surprisingly, wild type mouse bestrophin-4 (mBest4) did not induce functional Cl channels when over-expressed in HEK293 cells. However, deletion of part of the C-terminus (residues 353-669) produced large Cl currents, suggesting the presence of a C-terminal motif that inhibited Cl channel function. Deletion of a short motif (356-364) or substitution of certain residues in this motif with alanines also resulted in expression of robust Cl currents. The channel activity of the mBest4 protein lacking the C-terminus (residues 353-669) was specifically inhibited by co-expression of C-terminal fragments of mBest4 having the inhibitory motif, suggesting that the C-terminal motif blocked mBest4 channel activity probably by interacting with the channel pore. |
