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Review
. 2018 Feb 8;19(2):521.
doi: 10.3390/ijms19020521.

Plant and Mammal Aquaporins: Same but Different

Affiliations
Review

Plant and Mammal Aquaporins: Same but Different

Timothée Laloux et al. Int J Mol Sci. .

Abstract

Aquaporins (AQPs) constitute an ancient and diverse protein family present in all living organisms, indicating a common ancient ancestor. However, during evolution, these organisms appear and evolve differently, leading to different cell organizations and physiological processes. Amongst the eukaryotes, an important distinction between plants and animals is evident, the most conspicuous difference being that plants are sessile organisms facing ever-changing environmental conditions. In addition, plants are mostly autotrophic, being able to synthesize carbohydrates molecules from the carbon dioxide in the air during the process of photosynthesis, using sunlight as an energy source. It is therefore interesting to analyze how, in these different contexts specific to both kingdoms of life, AQP function and regulation evolved. This review aims at highlighting similarities and differences between plant and mammal AQPs. Emphasis is given to the comparison of isoform numbers, their substrate selectivity, the regulation of the subcellular localization, and the channel activity.

Keywords: aquaporins; gating; heteromerization; mammal; plant; regulation; specificity.

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Conflict of interest statement

The authors declare no conflict of interest.

References

    1. Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y. Structural determinants of water permeation through aquaporin-1. Nature. 2000;407:599–605. - PubMed
    1. Pao G.M., Wu L.F., Johnson K.D., Hofte H., Chrispeels M.J., Sweet G., Sandal N.N., Saier M.H., Jr. Evolution of the MIP family of integral membrane transport proteins. Mol. Microbiol. 1991;5:33–37. doi: 10.1111/j.1365-2958.1991.tb01823.x. - DOI - PubMed
    1. Preston G.M., Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family. Proc. Natl. Acad. Sci. USA. 1991;88:11110–11114. doi: 10.1073/pnas.88.24.11110. - DOI - PMC - PubMed
    1. De Groot B.L., Grubmuller H. Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF. Science. 2001;294:2353–2357. doi: 10.1126/science.1062459. - DOI - PubMed
    1. Tajkhorshid E., Nollert P., Jensen M.O., Miercke L.J., O’Connell J., Stroud R.M., Schulten K. Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science. 2002;296:525–530. doi: 10.1126/science.1067778. - DOI - PubMed

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