Role of CBS and Bateman Domains in Phosphorylation-Dependent Regulation of a CLC Anion Channel.

@article{Yamada2016RoleOC,
  title={Role of CBS and Bateman Domains in Phosphorylation-Dependent Regulation of a CLC Anion Channel.},
  author={Toshiki Yamada and M. Krzeminski and Z. Bozoky and J. Forman-Kay and K. Strange},
  journal={Biophysical journal},
  year={2016},
  volume={111 9},
  pages={
          1876-1886
        }
}
Eukaryotic CLC anion channels and transporters are homodimeric proteins composed of multiple α-helical membrane domains and large cytoplasmic C-termini containing two cystathionine-β-synthase domains (CBS1 and CBS2) that dimerize to form a Bateman domain. The Bateman domains of adjacent CLC subunits interact to form a Bateman domain dimer. The functions of CLC CBS and Bateman domains are poorly understood. We utilized the Caenorhabditis elegans CLC-1/2/Ka/Kb anion channel homolog CLH-3b to… Expand

References

SHOWING 1-10 OF 49 REFERENCES
Differential regulation of a CLC anion channel by SPAK kinase ortholog-mediated multisite phosphorylation.
A role for CBS domain 2 in trafficking of chloride channel CLC-5.
...
1
2
3
4
5
...