Aquaporins and Transport of Metalloids
Aquaporins or major intrinsic proteins (MIPs) are channels facilitating the passive diffusion of small uncharged solutes across biological membranes. In addition to water, several aquaporin isoforms were shown to transport gases (NH3 and CO2) or other uncharged solutes including metalloid compounds (arsenite, boric acid, silicic acid, selenite, and antimonite).
Aquaporin Discovery and Phylogeny
Aquaporins are membrane proteins belonging to the ancient major intrinsic protein (MIP) family whose members are found in all kingdoms of life. Although the term aquaporin was initially restricted to MIPs transporting water molecules, it is now used to describe all MIPs.
The first demonstration of the water channel activity of a MIP protein was published in 1992 when Peter Agre and coworkers heterologously expressed in Xenopus oocytes a 28-kDa protein (CHIP28) from human erythrocyte membrane...
- Bienert GP, Chaumont F (2011) Plant aquaporins: roles in water homeostasis, nutrition, and signaling processes. Springer, Berlin/HeidelbergGoogle Scholar
- Danielson JAH, Johanson U (2010) Phylogeny of major intrinsic proteins. Landes Bioscience-Springer, New YorkGoogle Scholar
- Hachez C, Chaumont F (2010) Aquaporins: a family of highly regulated multifunctional channels. Landes Bioscience-Springer, New YorkGoogle Scholar
- Ma JF (2010) Silicon transporters in higher plants. Landes Bioscience-Springer, New YorkGoogle Scholar