Elasmobranch Aqp10 paralogs differ in glycerol permeability
1School of Life Science and Technology, Institute of Science Tokyo, Yokohama, Japan.
Summary
Cartilaginous fish aquaglyceroporins (Aqp10) show unique evolutionary paths. Elasmobranch Aqp10C1 paralogs lost glycerol permeability after gene duplication, unlike other Aqp10 variants.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Aquaglyceroporins (Aqp) facilitate water and small solute transport.
- Knowledge of aquaglyceroporins in cartilaginous fish, especially Aqp10 paralogs, is limited.
- Understanding functional divergence in fish-specific paralogs is crucial.
Purpose of the Study:
- To investigate the evolutionary relationships of Aqp10 paralogs in cartilaginous fish.
- To compare the functional differences, specifically solute permeability, of these Aqp10 paralogs.
- To elucidate the evolutionary mechanisms driving Aqp10 divergence in elasmobranchs.
Main Methods:
- Molecular phylogenetic analysis
- Synteny analysis
- Gene duplication analysis
- Functional expression in Xenopus oocytes
- Solute permeability assays (swelling assays)
Main Results:
- Elasmobranch Aqp10 paralogs (Aqp10C1, Aqp10C2) originated from a cartilaginous fish-specific tandem gene duplication.
- Holocephalan species possess Aqp10 paralogs likely derived from Aqp10C2.
- Aqp10C2 maintained glycerol permeability, while Aqp10C1 exhibited significantly reduced glycerol permeability, resembling water-specific aquaporins.
Conclusions:
- Aqp10 function is highly differentiated in elasmobranchs following gene duplication.
- The Aqp10C1 paralog may have lost its glycerol permeability due to sub/neofunctionalization after tandem duplication.
- This study provides insights into the evolution of aquaglyceroporins in cartilaginous fish.
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