Redox regulation of the proteasome via S-glutathionylation
نویسندگان
چکیده
منابع مشابه
Redox regulation of the proteasome via S-glutathionylation☆
The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S core particle. The majority of these are flanked on one or both sides by regulatory units. Most c...
متن کاملRedox regulation of proteasome function
Reactive Oxygen Species (ROS) and Reactive Nitrogen Species (RNS) were initially regarded mainly as metabolic by-products with damaging properties. Over the last decade, our understanding of their role in metabolism was drastically changed and they were recognized as essential mediators in cellular signaling cascades, as well as modulators of biochemical pathways. Proteostasis is highly affecte...
متن کامل20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins.
Protein S-glutathionylation is a post-translational modification that controls many cellular pathways. Recently, we demonstrated that the α5-subunit of the 20S proteasome is S-glutathionylated in yeast cells grown to the stationary phase in rich medium containing glucose, stimulating 20S core gate opening and increasing the degradation of oxidized proteins. In the present study, we evaluated th...
متن کاملRegulation of neovascularization by S-glutathionylation via the Wnt5a/sFlt-1 pathway.
S-glutathionylation occurs when reactive oxygen or nitrogen species react with protein-cysteine thiols. Glutaredoxin-1 (Glrx) is a cytosolic enzyme which enzymatically catalyses the reduction in S-glutathionylation, conferring reversible signalling function to proteins with redox-sensitive thiols. Glrx can regulate vascular hypertrophy and inflammation by regulating the activity of nuclear fact...
متن کاملS-glutathionylation: a redox-sensitive switch participating in nitroso-redox balance.
Cysteine side chains of proteins are being increasingly appreciated as the site of major posttranslational modifications that exert profound degrees of protein regulation. One of the consequences of tissue nitroso-redox imbalance is a process by which regulatory thiols switch from a state of physiologic regulation by S-nitrosylation to a state of dysregulated function because of oxidation. A ke...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Redox Biology
سال: 2014
ISSN: 2213-2317
DOI: 10.1016/j.redox.2013.12.003