Function
Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane.[1]
- Aquaporin-0 functions as water channel in lens fibers.
- Aquaporin-1 see details in Aquaporin-1.
- Aquaporin-2 function is to reabsorb water from urine in the kidney.
- Aquaporin-3 function is to promote glycerol permeability across cell membrane.
- Aquaporin-4 regulates water balance in the central nervous system.
- Aquaporin-5 is implicated in the forming of saliva, tears and pulmonary secretions.
- Aquaporin-7 regulates nutrient availability and signaling responding to cellular stress[2]
- Aquaporin-10 is expressed exclusively in adipocytes and participates in maintaining low glycerol content in them[3]
- NIP-2 aquaporin Nodulin 26-like intrinsic protein is a plant Aquaporin[4]
- TIP-2 aquaporin is permeable to water and ammonia[5]
- Aquaporin-Z is a major water channel in bacteria.
- Aquaglycerolporin (GLpf) is a water channel which can transport glycerol, polyalcohols, urea and other small solutes.
Disease
Mutations 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 highlights
Aquaporins 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
Aquaporin 3D structures
- ↑ 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