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A short motif in the C‐terminus of mouse bestrophin 4 inhibits its activation as a Cl channel
Author(s) -
Qu Zhiqiang,
Cui Yuanyuan,
Hartzell Criss
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.025
Subject(s) - motif (music) , c terminus , hek 293 cells , chemistry , n terminus , biophysics , structural motif , microbiology and biotechnology , stereochemistry , biochemistry , peptide sequence , amino acid , biology , gene , physics , acoustics
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.