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SUMO: a (Oxidative) Stressed Protein

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Abstract

Redox species are produced during the physiological cellular metabolism of a normal tissue. In turn, their presence is also attributed to pathological conditions including neurodegenerative diseases. Many are the molecular changes that occur during the unbalance of the redox homeostasis. Interestingly, posttranslational protein modifications (PTMs) play a remarkable role. In fact, several target proteins are modified in their activation, localization, aggregation, and expression after the cellular stress. Among PTMs, protein SUMOylation represents a very important molecular modification pathway during “oxidative stress”. It has been reported that this ubiquitin-like modification is a fine sensor for redox species. Indeed, SUMOylation pathway efficiency is affected by the exposure to oxidative species in a different manner depending on the concentration and time of application. Thus, we here report updated evidence that states the role of SUMOylation in several pathological conditions, and we also outline the key involvement of c-Jun N-terminal kinase and small ubiquitin modifier pathway cross talk.

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Acknowledgments

We apologize to any colleague whose work may have inadvertently been omitted. RN is supported by the Italian Ministry of Education.

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The authors declare that there is no conflict of interest.

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Authors and Affiliations

  1. Laboratory of Pharmacology of Synaptic Plasticity, EBRI “Rita Levi-Montalcini” Foundation, Via del Fosso di Fiorano 64/65, 00143, Rome, Italy

    Marco Feligioni

  2. Department of Physiology and Pharmacology, Sapienza University of Rome, Rome, Italy

    Robert Nisticò

  3. Laboratory of Experimental Neurology, IRCCS Santa Lucia Foundation, Rome, Italy

    Robert Nisticò

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  1. Marco Feligioni
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  2. Robert Nisticò
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Correspondence to Marco Feligioni.

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Feligioni, M., Nisticò, R. SUMO: a (Oxidative) Stressed Protein. Neuromol Med 15, 707–719 (2013). https://doi.org/10.1007/s12017-013-8266-6

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  • DOI: https://doi.org/10.1007/s12017-013-8266-6

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