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 (DLE) 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.
Description
Targeting of vacuolar membrane localized members of the TPK channel family. - PubMed - NCBI
%0 Journal Article
%1 Dunkel:2008:Mol-Plant:19825594
%A Dunkel, M
%A Latz, A
%A Schumacher, K
%A Müller, T
%A Becker, D
%A Hedrich, R
%D 2008
%J Mol Plant
%K myown
%N 6
%P 938-949
%R 10.1093/mp/ssn064
%T Targeting of vacuolar membrane localized members of the TPK channel family
%U https://www.ncbi.nlm.nih.gov/pubmed/19825594
%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 (DLE) 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{Dunkel:2008:Mol-Plant:19825594,
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 (DLE) 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 = {2017-03-21T20:38:05.000+0100},
author = {Dunkel, M and Latz, A and Schumacher, K and M{\"u}ller, T and Becker, D and Hedrich, R},
biburl = {https://www.bibsonomy.org/bibtex/2f1637a875272f7d32e87758bfbecd459/dirkbecker},
description = {Targeting of vacuolar membrane localized members of the TPK channel family. - PubMed - NCBI},
doi = {10.1093/mp/ssn064},
interhash = {49ec5206bb85cff99e91e3b103fb187d},
intrahash = {f1637a875272f7d32e87758bfbecd459},
journal = {Mol Plant},
keywords = {myown},
month = nov,
number = 6,
pages = {938-949},
pmid = {19825594},
timestamp = {2017-03-21T20:38:05.000+0100},
title = {Targeting of vacuolar membrane localized members of the TPK channel family},
url = {https://www.ncbi.nlm.nih.gov/pubmed/19825594},
volume = 1,
year = 2008
}