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Cellular responses to stress are regulated by stress-activated protein kinases that are part of the mitogen-activated protein kinase (MAPK) family. Because each component in this signaling cascade has multiple downstream targets, key questions pertaining to the regulation of the stress response include understanding of the mechanisms underlying the duration of their activity, diversification of the signal to select downstream targets, and magnitude of the signal. Here, we summarize our current understanding of ubiquitin’s roles in dictating the type, strength, and specificity of MAPK signaling. Our summary suggests that ubiquitin serves as a key regulator of MAPK, an arrangement that may serve as a paradigm for other signal transduction pathways.