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.

Feligioni, M., Nistico', R.g. (2013). SUMO: A (Oxidative) Stressed Protein. NEUROMOLECULAR MEDICINE, 15(4), 707-719 [10.1007/s12017-013-8266-6].

SUMO: A (Oxidative) Stressed Protein

NISTICO', ROBERT GIOVANNI
2013-01-01

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.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/14
English
Animals; Diabetes Mellitus; Humans; JNK Mitogen-Activated Protein Kinases; MAP Kinase Signaling System; Neoplasm Proteins; Neoplasms; Nerve Tissue Proteins; Neurodegenerative Diseases; Oxidation-Reduction; Oxidative Stress; Reactive Oxygen Species; Signal Transduction; Small Ubiquitin-Related Modifier Proteins; Sumoylation; Ubiquitin; Ubiquitin-Protein Ligase Complexes
Feligioni, M., Nistico', R.g. (2013). SUMO: A (Oxidative) Stressed Protein. NEUROMOLECULAR MEDICINE, 15(4), 707-719 [10.1007/s12017-013-8266-6].
Feligioni, M; Nistico', Rg
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/133148
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