@article{RN1142,
  abstract = {Four members of the tandem-pore potassium channel family of Arabidopsis thaliana (TPK1, 2, 3, and 5) reside in the vacuolar membrane, whereas TPK4 is a plasma membrane K+-channel. By constructing chimeras between TPK1 and TPK4, we attempted to identify channel domains involved in the trafficking process and found that the TPK1 cytoplasmic C-terminal domain (CT) is critical for the ER- as well as Golgi-sorting steps. Following site-directed mutagenesis, we identified a diacidic motif (IDLE) required for ER-export of TPK1. However, this diacidic motif in the C-terminus is not conserved among other members of the TPK family, and TPK3 sorting is independent of its CT. Moreover, the 14-3-3 binding site of TPK1, essential for channel activation, is not involved in channel sorting.},
  added-at = {2024-02-14T14:38:32.000+0100},
  author = {Dunkel, M. and Latz, A. and Schumacher, K. and Wüller, T. and Becker, D. and Hedrich, R.},
  biburl = {https://www.bibsonomy.org/bibtex/21ff9b22f4f7dda293f36a8ec2896842e/rainerhedrich_2},
  doi = {10.1093/mp/ssn064},
  interhash = {bd228c2343316358fac57c7a3436fde6},
  intrahash = {1ff9b22f4f7dda293f36a8ec2896842e},
  issn = {1674-2052},
  journal = {Molecular Plant},
  keywords = {fluorescent green myOwn protein},
  note = {400hg
Times Cited:67
Cited References Count:82},
  number = 6,
  pages = {938-949},
  timestamp = {2024-02-14T14:38:32.000+0100},
  title = {Targeting of Vacuolar Membrane Localized Members of the TPK Channel Family},
  type = {Journal Article},
  url = {/brokenurl#<Go to ISI>://WOS:000262858000006},
  volume = 1,
  year = 2008
}