Oxidized lipids in plants comprise a variety of reactive electrophiles that contain an alpha,beta-unsaturated carbonyl group. While some of these compounds are formed enzymatically, many of them are formed by non-enzymatic pathways. In addition to their chemical reactivity/toxicity low levels of these compounds are also biologically active. Despite their structural diversity and biosynthetic origin, common biological activities such as induction of defense genes, activation of detoxification responses and growth inhibition have been documented. However, reactive electrophilic oxylipins are poorly defined as a class of compounds but have at least two properties in common, i.e., lipophilicity and thiol-reactivity. Thiol-reactivity is a property of reactive oxylipins (RES) shared by reactive oxygen and nitrogen species (ROS and RNS) and enables these agents to modify proteins in vivo. Thiol-modification is assumed to represent a key mechanism involved in signal transduction. A metaanalysis of proteomic studies reveals that RES oxylipins, ROS and RNS apparently chemically modify a similar set of highly sensitive proteins, virtually all of which are targets for thioredoxins. Moreover, most of these proteins are redox-regulated, i.e., posttranslational thiol-modification alters the activity or function of these proteins. On the transcriptome level, effects of RES oxylipins and ROS on gene induction substantially overlap but are clearly different. Besides electrophilicity other structural properties such as target affinity apparently determine target selectivity and biological activity. In this context, different signalling mechanisms and signal transduction components identified in plants and non-plant organisms as well as putative functions of RES oxylipins are discussed.