Small ubiquitin-like modifier (SUMO) is a small (∼12kDa) protein that occurs in all eukaryotes and participates in the reversible posttranslational modification of target cellular proteins. The three-dimensional structure of SUMO and ubiquitin (Ub) are superimposable although there is very little similarity in their primary amino acid sequences. In all organisms, conjugation and deconjugation of Ub and SUMO proceed by the same reactions while using pathway-specific enzymes. SUMO conjugation in plants is a part of the controls governing important biological processes such as growth, development, flowering, environmental (abiotic) stress responses, and response to pathogen infection. Most of the evidence for this comes from genetic analyses. Recent efforts to dissect the function of sumoylation have focused on uncovering targets of SUMO conjugation by using either a yeast two-hybrid screen employing components of the SUMO cycle as bait or by using affinity purification of SUMO-conjugated proteins followed by identification of these proteins by mass spectrometry. This chapter reviews the current knowledge regarding sumoylation in plants, with special focus on the model plant Arabidopsis thaliana.