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Voltage‐gating of aquaporins, a putative conserved safety mechanism during ionic stresses
FEBS Letters ( IF 3.0 ) Pub Date : 2020-10-17 , DOI: 10.1002/1873-3468.13944
Robin Mom 1 , Beatriz Muries 1 , Pierrick Benoit 1 , Julien Robert-Paganin 2 , Stéphane Réty 3 , Jean-Stéphane Venisse 1 , Agilio Padua 4 , Philippe Label 1 , Daniel Auguin 5
Affiliation  

Aquaporins are transmembrane water channels found in almost every living organism. Numerous studies have brought a good understanding of both water transport through their pores and the regulations taking place at the molecular level, but subtleties remain to be clarified. Recently, a voltage‐related gating mechanism involving the conserved arginine of the channel’s main constriction was captured for human aquaporins through molecular dynamics studies. With a similar approach, we show that this voltage‐gating could be conserved among this family and that the underlying mechanism could explain part of plant AQPs diversity when contextualized to high ionic concentrations provoked by drought. Finally, we identified residues as adaptive traits which constitute good targets for drought resistance plant breeding research.

中文翻译:

水通道蛋白的电压门控,一种在离子应力下假定的保守安全机制

水通道蛋白是几乎在所有生物体中都能发现的跨膜水通道。许多研究已经很好地理解了水通过它们的孔隙运输和分子水平上发生的调节,但仍有待澄清的微妙之处。最近,通过分子动力学研究为人类水通道蛋白捕获了一种与电压相关的门控机制,该机制涉及通道主要收缩的保守精氨酸。使用类似的方法,我们表明这种电压门控在这个家族中是保守的,并且当干旱引起的高离子浓度背景下,潜在的机制可以解释部分植物 AQP 的多样性。最后,我们将残留物确定为适应性性状,这些性状构成了抗旱植物育种研究的良好目标。
更新日期:2020-10-17
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