期刊
MOLECULAR PLANT
卷 1, 期 6, 页码 938-949出版社
OXFORD UNIV PRESS
DOI: 10.1093/mp/ssn064
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-
资金
- Deutsche Forschungsgemeinschaft [SFB487]
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.
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