Low-molecular-weight glutenin subunits (LMW-GS) are polymeric protein components of wheat endosperm and like all seed storage proteins, are digested to provide nutrients for the embryo during seed germination and seedling growth. Due to their structural characteristics, they exhibit features important for the technological properties of wheat flour. Their ability to form inter-molecular disulphide bonds with each other and/or with high-molecular-weight glutenin subunits (HMW-GS), is important for the formation of the glutenin polymers, which are among the biggest macromolecules present in nature, and determine the processing properties of wheat dough. Explanation of the structural basis for these correlations continues to intrigue researchers and, while earlier emphasis had been on HMW-GS, considerable attention is now being focused on the LMW-GS.LMW-GS are a highly polymorphic protein complex, including proteins with gliadin-type sequences. Difficulty in separating single components, arising from the complexity of the group, has limited the characterisation of the individual proteins and the establishment of clear-cut relationships with quality parameters.Here we review results concerning different aspects of LMW-GS, including their structural characteristics, genetic control, and relationships with quality parameters. In addition, we emphasise the distinction between the components with sequences unique to the LMW-GS fraction and those behaving like glutenin subunits (incorporated into polymers), but with sequences corresponding to gliadins.