The history of the water channel and recent structural and functional analy
ses of aquaporins are reviewed, These ubiquitous channels are important for
bacteria, plants and animals, exhibit a pronounced sequence homology and s
hare functional as well as structural similarities. Aquaporins allow water
or small specific solutes to pass unhindered, but black the passage of ions
to prevent dissipation of the transmembrane potential. Besides advances in
structure determination, recent experiments suggest that many of these cha
nnels are regulated by pH variations, phosphorylation and binding of auxili
ary proteins.