AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin

TL;DR

This study reveals that AQP1, traditionally known as a water channel, also influences cell migration by interacting with Lin-7 and beta-catenin, indicating a broader physiological role beyond water transport.

Contribution

The paper uncovers a novel intracellular role of AQP1 in cell migration through its interaction with Lin-7 and beta-catenin, expanding understanding of AQP1 functions.

Findings

AQP1 silencing impairs cell migration and F-actin organization.

AQP1 co-immunoprecipitates with Lin-7, indicating interaction.

Knockdown of AQP1 reduces Lin-7 and beta-catenin levels.

Abstract

Background: AQP1 belongs to aquaporins family, water-specific, membrane-channel proteins expressed in diverse tissues. Recent papers showed that during angiogenesis, AQP1 is expressed preferentially by microvessels, favoring angiogenesis via the increase of permeability In particular, in AQP1 null mice, endothelial cell migration is impaired without altering their proliferation or adhesion. Therefore, AQP1 has been proposed as a novel promoter of tumor angiogenesis. Methods/Findings: Using targeted silencing of AQP1 gene expression, an impairment in the organization of F-actin and a reduced migration capacity was demonstrated in human endothelial and melanoma cell lines. Interestingly, we showed, for the first time, that AQP1 co-immunoprecipitated with Lin-7. Lin7-GFP experiments confirmed co-immunoprecipitation. In addition, the knock down of AQP1 decreased the level of expression of Lin-7 and b-catenin and the inhibition of proteasome contrasted partially such a decrease. Conclusions/Significance: All together, our findings show that AQP1 plays a role inside the cells through Lin-7/b-catenin interaction. Such a role of AQP1 is the same in human melanoma and endothelial cells, suggesting that AQP1 plays a global physiological role. A model is presented.