Abstract
Sumoylation is the covalent attachment of the small ubiquitin-related modifier (SUMO) to a vast variety of proteins in order to modulate their function. Sumoylation has emerged as an important modification with a regulatory role in the cellular response to different types of stress including osmotic, hypoxic and oxidative stress. Hypoxia can occur under physiological or pathological conditions, such as ischemia and cancer, as a result of an oxygen imbalance caused by low supply and/or increased consumption. The hypoxia inducible factors (HIFs), and the proteins that regulate their fate, are critical molecular mediators of the response to hypoxia and modulate procedures such as glucose and lipid metabolism, angiogenesis, erythropoiesis and, in the case of cancer, tumor progression and metastasis. Here, we provide an overview of the sumoylation-dependent mechanisms that are activated under hypoxia and the way they influence key players of the hypoxic response pathway. As hypoxia is a hallmark of many diseases, understanding the interrelated connections between the SUMO and the hypoxic signaling pathways can open the way for future molecular therapeutic interventions.
Highlights
Post-translational modifications are critical events in cellular signaling that allow regulation and fine-tuning of protein function
Sumoylation of RanGAP1 is required for its localization at the nuclear pore complexes and its interaction with RanBP2, which is essential for the role of RanGAP1 in the protein nuclear import [4,5]
Sumoylation of proteins contribute to most aspects of cell biology
Summary
Post-translational modifications are critical events in cellular signaling that allow regulation and fine-tuning of protein function. Sumoylation is a post-translational modification that involves the covalent attachment of the 97-amino acid SUMO (small ubiquitin-like modifier) protein to lysine residues of target proteins [1,2,3]. Studies over the years revealed that SUMO targets control nuclear transport mechanisms but rather participate in most aspects of cell biology and sumoylation has been established as one of the most common reversible protein modifications implicated in cellular processes ranging from signal transduction and ion transport to transcription, recombination and chromosome segregation and DNA repair [7,8]. We will focus on the SUMO modifications that are implicated in the cellular adaptation to hypoxia and will highlight the significance of sumoylation targeting factors of the hypoxia signaling pathway
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