Mutations at key pore-lining positions differentiate the water permeability of fish lens aquaporin from other vertebrates |
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Authors: | Luisa Calvanese Romina Oliva |
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Affiliation: | a Department of Chemistry, University “Federico II” of Naples, Via Cintia 45, I-80126, Naples, Italy b EMBL/EBI, The Wellcome Trust Genome Campus, CB10 1SD, Hinxton, Cambridge, United Kingdom c Department of Applied Sciences, University “Parthenope” of Naples, Centro Direzionale Isola C4, I-80143, Naples, Italy |
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Abstract: | Aquaporin-0 (AQP0) is the major integral membrane protein of lens fiber cell and helps to maintain lens transparency by mediating inter-cell adhesion. To shed light on the unexpected higher water transport efficiency of killifish AQP0 as compared to mammalian orthologues, we performed a comparative analysis of all available AQP0 sequences and built 3D-models for representatives of different vertebrate classes.The analysis shows that air-living organisms evolved specific mutations at pore-lining positions to modulate the AQP0 water transport efficiency while maintaining the correct tertiary/quaternary arrangement to allow the formation of “thin junctions” between lens fiber cells. We conclude that the low permeability of mammalian AQP0 is required not to promote cell adhesion, but to modulate the water balance in a dry environment. |
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Keywords: | Aquaporin-0 Water transport Comparative analysis Molecular modeling Adaptive evolution Fish vision |
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