ArticlePlant signaling & behavior2015
The LxxxA motif in the third transmembrane helix of the maize aquaporin ZmPIP2;5 acts as an ER export signal.
Article in Plant signaling & behavior, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Tales of tails in transporters.Open biology · 2019Review
- Transmembrane Helices 2 and 3 Determine the Localization of Plasma Membrane Intrinsic Proteins in Eukaryotic Cells.Frontiers in plant science · 2019Article
- Plant and Mammal Aquaporins: Same but Different.International journal of molecular sciences · 2018Review
- Heterotetramerization of Plant PIP1 and PIP2 Aquaporins Is an Evolutionary Ancient Feature to Guide PIP1 Plasma Membrane Localization and Function.Frontiers in plant science · 2018Article
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2 authors.
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Abstract
The subcellular localization of aquaporins belonging to the plasma membrane intrinsic protein (PIP) subfamily is highly regulated. In maize (Zea mays), ZmPIP1s are retained in the endoplasmic reticulum (ER) whereas ZmPIP2s are able to reach the plasma membrane (PM). We recently identified a new sorting determinant which is buried within the third transmembrane domain (TM3) of ZmPIP2;5. The Leu127 and Ala131 are required for the localization of ZmPIP2;5 in the PM and for its exit from the ER. However, when inserted into ZmPIP1;2, these amino acids were not sufficient to export the protein out of the ER. Here, we show that, when inserted into a truncated version of ZmPIP1;2 consisting only of its TM3 region, Leu127 and Ala131 of ZmPIP2;5 are able to partially bring the protein to the PM, demonstrating the active anterograde sorting function of this motif.
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