Targeting of vacuolar membrane localized members of the TPK channel family
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 pro...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
6 November 2008
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| In: |
Molecular plant
Year: 2008, Volume: 1, Issue: 6, Pages: 938-949 |
| ISSN: | 1752-9867 |
| DOI: | 10.1093/mp/ssn064 |
| Online Access: | Verlag, Volltext: http://dx.doi.org/10.1093/mp/ssn064 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S1674205214604512 
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| Author Notes: | Marcel Dunkel, Andreas Latz, Karin Schumacher, Thomas Müller, Dirk Becker, Rainer Hedrich |
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| 520 | |a 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. | ||
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