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.
%0 Journal Article
%1 RN1142
%A Dunkel, M.
%A Latz, A.
%A Schumacher, K.
%A Wüller, T.
%A Becker, D.
%A Hedrich, R.
%D 2008
%J Molecular Plant
%K fluorescent green myOwn protein
%N 6
%P 938-949
%R 10.1093/mp/ssn064
%T Targeting of Vacuolar Membrane Localized Members of the TPK Channel Family
%U /brokenurl#<Go to ISI>://WOS:000262858000006
%V 1
%X 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.
@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
}