A Critical Role for ISGylation, Ubiquitination and, SUMOylation in Brain Damage: Implications for Neuroprotection.

A Critical Role for ISGylation, Ubiquitination and, SUMOylation in Brain Damage: Implications for Neuroprotection. Neurochem Res. 2020 Jun 04;: Authors: Nakka VP, Mohammed AQ Abstract Post-translational modification (PTMs) of proteins by ubiquitin and ubiquitin-like modifiers such as interferon-stimulated gene 15 (ISG15) and small ubiquitin-related modifier (SUMO) play a critical role in the regulation of brain pathophysiology. Protein ISGylation is a covalent attachment of ISG15 to its target proteins, which is a unique PTM among other ubiquitin-like modifiers. Although, ISG15 shares sequence homology to ubiquitin, yet the functional significance of protein ISGylation is distinct from ubiquitination and SUMOylation. Further, ISG15 highly conserved among vertebrate species, unlike the other ubiquitin-like modifiers. ISGylation modulates various intracellular mechanisms such as Janus kinase/signal transducers and activators of transcription (JAK-STAT) pathway, autophagy, DNA repair, etc., indicating its biological significance. ISGylation emerged as one of the important mechanisms in the regulation of various neurological disorders including stroke, traumatic brain injury (TBI), basal ganglia calcification, and ataxia-telangiectasia. It appears that protein ISGylation is an endogenous neuroprotective mechanism. This review discusses the role of ISGylation in various brain pathologies with a particular emphasis on cerebral ischemia/str...
Source: Neurochemical Research - Category: Neuroscience Authors: Tags: Neurochem Res Source Type: research