ArticleBiochemistry2009
Site-specific methionine oxidation initiates calmodulin degradation by the 20S proteasome.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Acceleration of Protein Degradation by 20S Proteasome-Binding Peptides Generated by In Vitro Artificial Evolution.International journal of molecular sciences · 2023Article
- Accurate Proteomewide Measurement of Methionine Oxidation in Aging Mouse Brains.Journal of proteome research · 2022Article
- Decreased proteasomal cleavage at nitrotyrosine sites in proteins and peptides.Redox biology · 2021Article
- Met125 is essential for maintaining the structural integrity of calmodulin's C-terminal domain.Scientific reports · 2020Article
- Resolved Structural States of Calmodulin in Regulation of Skeletal Muscle Calcium Release.Biophysical journal · 2020Article
- Quantitative Analysis of in Vivo Methionine Oxidation of the Human Proteome.Journal of proteome research · 2020Article
- Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.Protein science : a publication of the Protein Society · 2019Article
- Oxidative Post-translational Modifications Accelerate Proteolytic Degradation of Calprotectin.Journal of the American Chemical Society · 2018Article
- Redox regulation of the actin cytoskeleton and its role in the vascular system.Free radical biology & medicine · 2017Review
- Calcium-Dependent Structural Dynamics of a Spin-Labeled RyR Peptide Bound to Calmodulin.Biophysical journal · 2016Article
- Oxidation increases the strength of the methionine-aromatic interaction.Nature chemical biology · 2016Article
- Impact of methionine oxidation on calmodulin structural dynamics.Biochemical and biophysical research communications · 2015Article
- Article
- Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014Article
- Biochemical characterization and role of the proteasome in the oxidative stress response of adult Schistosoma mansoni worms.Parasitology research · 2014Article
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- The ubiquitin-proteasome system in retinal health and disease.Molecular neurobiology · 2013Review
- Roles for the ubiquitin-proteasome pathway in protein quality control and signaling in the retina: implications in the pathogenesis of age-related macular degeneration.Molecular aspects of medicine · 2012Review
- Adaptive response, evidence of cross-resistance and its potential clinical use.International journal of molecular sciences · 2012Review
- Structural and functional impact of site-directed methionine oxidation in myosin.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The proteasome is a key intracellular protease that regulates processes, such as signal transduction and protein quality control, through the selective degradation of specific proteins. Signals that target a protein for degradation, collectively known as degrons, have been defined for many proteins involved in cell signaling. However, the molecular signals involved in recognition and degradation of proteins damaged by oxidation have not been completely defined. The current study used biochemical and spectroscopic measurements to define the properties in calmodulin that initiate degradation by the 20S proteasome. Our experimental approach involved the generation of multiple calmodulin mutants with specific Met replaced by Leu. This strategy of site-directed mutagenesis permitted site-selective oxidation of Met to Met sulfoxide. We found that the oxidation-induced loss of secondary structure, as measured by circular dichroism, correlated with the rate of degradation for wild-type and mutants containing Leu substitutions in the C-terminus. However, no degradation was observed for mutants with Met to Leu substitution in the N-terminus, suggesting that oxidation-induced structural unfolding in the N-terminal region is essential for degradation by the 20S proteasome. Experiments comparing the thermodynamic stability of CaM mutants helped to further localize the critical site of oxidation-induced focal disruption between residues 51 and 72 in the N-terminal region. This work brings new biochemical and structural clarity to the concept of the degron, the portion of a protein that determines its susceptibility to degradation by the proteasome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.