Aquaporin
From Proteopedia
FunctionAquaporins are channel producing proteins which regulate the flow of water across the cell membrane.[1]
DiseaseMutations in aquaporin-2 cause diabitis insipidus. Mutations in aquaporin-0 in mice cause congenital cataracts. Aquaporin-4 is the primary autoimmune target of neuromyelitis optica. Structural highlightsAquaporins are made of α-helix bundles. The water transporting channel contains 2 restriction sites conferring an hourglass model to the channel. Two NPA motifs from opposite surfaces form one restriction. Another restriction is formed by a cluster of aromatic/arginine side chains which serves to weaken the hydrogen bonding between water molecules. 3D Structures of Aquaporin
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References
- ↑ Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 2003 Nov 27;555(1):72-8. PMID:14630322
- ↑ Dai C, Charlestin V, Wang M, Walker ZT, Miranda-Vergara MC, Facchine BA, Wu J, Kaliney WJ, Dovichi NJ, Li J, Littlepage LE. Aquaporin-7 Regulates the Response to Cellular Stress in Breast Cancer. Cancer Res. 2020 Oct 1;80(19):4071-4086. PMID:32631905 doi:10.1158/0008-5472.CAN-19-2269
- ↑ Laforenza U, Scaffino MF, Gastaldi G. Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. PLoS One. 2013;8(1):e54474. PMID:23382902 doi:10.1371/journal.pone.0054474
- ↑ Beamer ZG, Routray P, Choi WG, Spangler MK, Lokdarshi A, Roberts DM. Aquaporin family lactic acid channel NIP2;1 promotes plant survival under low oxygen stress in Arabidopsis. Plant Physiol. 2021 Dec 4;187(4):2262-2278. PMID:34890456 doi:10.1093/plphys/kiab196
- ↑ Lindahl V, Gourdon P, Andersson M, Hess B. Permeability and ammonia selectivity in aquaporin TIP2;1: linking structure to function. Sci Rep. 2018 Feb 14;8(1):2995. PMID:29445244 doi:10.1038/s41598-018-21357-2
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