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The key role of ubiquitination and sumoylation in signaling and cancer

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Ubiquitination and Sumoylation are two important posttranslational modifications that play pivotal roles in a variety of biological functions. Although Ubiquitination is traditionally viewed as a critical mark targeting proteins for proteasome-dependent degradation, recent studies reveal that it also plays ...

Ubiquitination and Sumoylation are two important posttranslational modifications that play pivotal roles in a variety of biological functions. Although Ubiquitination is traditionally viewed as a critical mark targeting proteins for proteasome-dependent degradation, recent studies reveal that it also plays nonproteolytic functions. In contrast, Sumoylation is long thought not to target proteins for degradation, accumulating evidence suggests that it can serve a priming effect prerequisite for ubiquitination, thereby inducing protein ubiquitination and degradation. Thus, there is an important cross-talk between sumoylation and ubiquitination in determining protein fate. Deregulation in these two marks may cause aberrant activity of proteins and in turn contributes to cancer development. In this Research Topic, we accept review articles, perspectives, research articles covering any one or both of these two posttranslational modifications in regulating diverse signal transduction pathways and providing the novel insights in unraveling the puzzle as to how they may regulate cancer progression and metastasis.


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