CONICET | Buscador de Institutos y Recursos Humanos

The functions of aquaporins (AQPs) are as wide as their presence in cells and tissues of organisms from all living Kingdoms [1]. Several regulatory and gating mechanisms have been described in different members of the family. It was recently demonstrated that human AQP1 (hAQP1) closes when membrane tension (T) increases [2]. In this work we proposed to study the mechanosensitive properties of PIP2 and TIP2, both AQPs from the plant B. vulgaris. Since these AQPs have different functional characteristics, and since their sequences show differences in some putative mechanosensitive sites, the purpose of this work is to elucidate whether these two AQPs have dissimilar functional responses to changes in , and if such possible differences are related to their distinct sequences. Preliminary results show that PIP2 responds in a similar way as hAQP1 to  increments. This is interesting because hAQP1 and PIP2 show high homology in their sequence. However, the sequence of TIP2 shows differences in some glycines, which could be putative sensors of mechanical gating.