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One of the aspects of insect osmoregulation that has most intrigued researchers is the ability of a simple tubular epithelium, such as the Malpighian tubule, to create both hypo- and hyperosmotic urine. Indeed, Ramsay's initial observation that isolated tubules could secrete a hypoosmotic urine led him to attribute the phenomenon to the active transport of water. In the ensuing decades several models for solute recycling have been proposed, but only in the last 15 years has it become clear that tubule water permeability is due to the presence of aquaporins (AQPs), the ubiquitous water transport proteins. There are 13 known human AQPs, and they are tissue and even membrane specific. It is now clear that the number and type of AQPs within a membrane are the major determinants of its water transport capacity. There are many gene homologs for the AQPs, so proof of function requires expression of the protein in a defined system. Within the insects, only seven AQPs have been functionally expressed and, of these, four directly or indirectly function in excretion. In this paper we review the basic structure and general function of AQPs and then examine the source, localization and functional attributes of those isolated from insects.

The role of aquaporins in excretion in insects