The glutathione transferases (glutathione S-transferases, GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione to an electrophilic substrate. Relatively little is known about the endogenous substrates of mosquito GSTs, and most studies have focused on their role in insecticide metabolism, because elevated levels of GST activity have been associated with resistance to all the major classes of insecticides. In addition, there is growing interest in the role of this enzyme family in maintaining the redox status of the mosquito cell, particularly in relation to vectorial capacity. Most GSTs are cytosolic dimeric proteins, although a smaller class of microsomal GSTs exists in insects, mammals, and plants. Each GST subunit has a G site that binds glutathione and a substrate-binding site or H site. There are more than 30 GST genes in mosquitoes. Additional diversity is contributed by alternative splicing to produce GSTs with differing substrate specificities. In this review, we first discuss the diversity of insect GST enzymes and their mode of action before focusing on the various functions that have been attributed to specific mosquito GSTs.