Redox signaling directly regulates TDP-43 via cysteine oxidation and disulfide cross-linking
نویسندگان
چکیده
Review timeline: Submission date: 10 February 2011 Editorial Decision: 02 March 2011 Additional correspondence (author): 03 March 2011 Additional correspondence (editor): 04 March 2011 Additional correspondence (author): 04 March 2011 Resubmission: 22 August 2011 Editorial Decision: 23 September 2011 Revision received: 25 October 2011 Editorial Decision: 28 November 2011 Revision received: 30 November 2011 Accepted: 30 November 2011
منابع مشابه
Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking.
TDP-43 is the major disease protein in ubiquitin-positive inclusions of amyotrophic lateral sclerosis and frontotemporal lobar degeneration (FTLD) characterized by TDP-43 pathology (FTLD-TDP). Accumulation of insoluble TDP-43 aggregates could impair normal TDP-43 functions and initiate disease progression. Thus, it is critical to define the signalling mechanisms regulating TDP-43 since this cou...
متن کاملEngineered pathways for correct disulfide bond oxidation.
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation. By linking correct disulfide bond formation to antibiotic resistance, we selected mutants that catalyze correct disulfide formation in the absence of DsbC, Escherichia coli's PDI. Most of our mut...
متن کاملA Peroxidase Peroxiredoxin 1-Specific Redox Regulation of the Novel FOXO3 microRNA Target let-7
Precision in redox signaling is attained through posttranslational protein modifications such as oxidation of protein thiols. The peroxidase peroxiredoxin 1 (PRDX1) regulates signal transduction through changes in thiol oxidation of its cysteines. We demonstrate here that PRDX1 is a binding partner for the tumor suppressive transcription factor FOXO3 that directly regulates the FOXO3 stress res...
متن کاملPotential role of glutathione in evolution of thiol-based redox signaling sites in proteins
Cysteine is susceptible to a variety of modifications by reactive oxygen and nitrogen oxide species, including glutathionylation; and when two cysteines are involved, disulfide formation. Glutathione-cysteine adducts may be removed from proteins by glutaredoxin, whereas disulfides may be reduced by thioredoxin. Glutaredoxin is homologous to the disulfide-reducing thioredoxin and shares similar ...
متن کاملCysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control.
Redox mechanisms function in control of gene expression, cell proliferation, and apoptosis, but the circuitry for redox signaling remains unclear. Cysteine and methionine are the only amino acids in proteins that undergo reversible oxidation/reduction under biologic conditions and, as such, provide a means for control of protein activity, protein-protein interaction, protein trafficking, and pr...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2011