Raw proteomics data.xlsx

Protein SUMOylation, where the addition of SUMO covalently modifies proteins, is a key regulatory mechanism in several cellular processes. This modification has multiple consequences: it can alter protein localization or interaction with other proteins or the stability and homeostasis of targets. MonoSUMOylation, wherein a single moiety of SUMO is added to proteins, generally alters the interaction properties of the target and, therefore, influences the sub-cellular localization of targets or supports the recruitment of new partners to processes. PolySUMOylation, where conjugated SUMO chains are formed, is involved in protein homeostasis. A class of enzymes, the SUMO-dependent ubiquitin ligases, recognize these polySUMOylated proteins and target them for proteasomal degradation.In this work, we studied the SUMOylation-protein homeostasis axis in <i>Candida glabrata</i> and established that regulated protein SUMOylation-deSUMOylation is critical to maintain protein homeostasis and any perturbation reduces the fitness and capacity of <i>Candida glabrata</i> to infect host cells.