کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2050841 | 1074182 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A short motif in the C-terminus of mouse bestrophin 4 inhibits its activation as a Cl channel A short motif in the C-terminus of mouse bestrophin 4 inhibits its activation as a Cl channel](/preview/png/2050841.png)
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.
Journal: FEBS Letters - Volume 580, Issue 8, 3 April 2006, Pages 2141–2146