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1 Departments of Medicine and Physiology, Cardiovascular Research Institute, University of California, San Francisco 94143-0521; and 2 Department of Cell Biology, the Scripps Research Institute, La Jolla, California 92037
The
aquaporins (AQPs) are a family of small membrane-spanning proteins
(monomer size ~30 kDa) that are expressed at plasma membranes in many
cells types involved in fluid transport. This review is focused on the
molecular structure and function of mammalian aquaporins. Basic
features of aquaporin structure have been defined using mutagenesis,
epitope tagging, and spectroscopic and freeze-fracture electron
microscopy methods. Aquaporins appear to assemble in membranes as
homotetramers in which each monomer, consisting of six
membrane-spanning 
-helical domains with cytoplasmically oriented amino and carboxy termini, contains a distinct water pore.
Medium-resolution structural analysis by electron cryocrystallography
indicated that the six tilted helical segments form a barrel
surrounding a central pore-like region that contains additional protein
density. Several of the mammalian aquaporins (e.g., AQP1, AQP2, AQP4,
and AQP5) appear to be highly selective for the passage of water, whereas others (recently termed aquaglyceroporins) also transport glycerol (e.g., AQP3 and AQP8) and even larger solutes (AQP9). Evidence
for possible movement of ions and carbon dioxide through the aquaporins
is reviewed here, as well as evidence for direct regulation of
aquaporin function by posttranslational modification such as
phosphorylation. Important unresolved issues include definition of the
molecular pathway through which water and solutes move, the nature of
monomer-monomer interactions, and the physiological significance of
aquaporin-mediated solute movement. Recent results from knockout mice
implicating multiple physiological roles of aquaporins suggest that the
aquaporins may be suitable targets for drug discovery by
structure-based and/or high-throughput screening strategies.
water transport; protein structure; electron microscopy; crystallography; water permeability
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