Abstract
EDITORIAL article Front. Oncol., 05 December 2012 | https://doi.org/10.3389/fonc.2012.00187
Highlights
Ubiquitination and sumoylation are two important posttranslational modifications that play pivotal roles in signaling regulation, protein trafficking, protein stability, and transcriptional regulation, regulating a plethora of biological processes such as cell survival, cell migration, DNA damage response (DDR), neurodegeneration, and cancer
Ubiquitination is traditionally viewed as a critical mark targeting proteins for proteasome-dependent degradation, recent studies have revealed that it has non-proteolytic functions
There is an important cross-talk between sumoylation and ubiquitination in determining protein fate. Deregulation in these two processes may cause aberrant activity of proteins and in turn contributes to cancer development. In this Research Topic, we assembled 10 review articles to discuss the role of these two post-translational modifications in regulating diverse signal transduction pathways, thereby providing novel insights in unraveling the puzzle as to how they may regulate cancer progression
Summary
The key role of ubiquitination and sumoylation in signaling and cancer: a research topic
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