ArticleMolecular biology of the cell2004
Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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Who cites it
121 citing papers in PubMed, 297 citations in OpenAlex.
- Redox cycling of viral RNA polymerase controls picornavirus replication.Nature communications · 2026Article
- Txnrd2 loss in skeletal muscle causes muscle atrophy and drives leanness and obesity resistance.Redox biology · 2026Article
- Chiral methionine oxidation reagents reveal stereospecific proteome modifications.bioRxiv : the preprint server for biology · 2026Article
- Yippee-like protein Moh1 links gene expression to metabolism and selective stress resistance inMicrobial cell (Graz, Austria) · 2026Article
- Identification of genetic variants associated with ear length in drop-eared dogs.Scientific reports · 2025Article
- Oxidative modification of methionine residue in α-synuclein by dopamine induces cellular vulnerability, oligomerization and secretion of α-synuclein.Journal of clinical biochemistry and nutrition · 2025Article
- Tissue-specific molecular regulation of aging mechanisms with methionine restriction in mice and the potential role of methionine sulfoxide reductase.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025Article
- MSRB3 antioxidant activity is necessary for inner ear cuticular plate structure and hair bundle integrity.Disease models & mechanisms · 2025Article
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Dynamic proximity interaction profiling suggests that YPEL2 is involved in cellular stress surveillance.Protein science : a publication of the Protein Society · 2024Article
- Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023Review
- Sulfur Amino Acid Restriction alters mitochondrial function depending on tissue, sex, and Methionine sulfoxide reductase A (MsrA) status.Research square · 2023Article
- Ndufaf2, a protein in mitochondrial complex I, interactsRedox report : communications in free radical research · 2023Article
- The transcriptome signature analysis of the epithelial-mesenchymal transition and immune cell infiltration in colon adenocarcinoma.Scientific reports · 2023Article
- Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023Article
- Response to oxidative stress of AML12 hepatocyte cells with knockout of methionine sulfoxide reductases.Free radical biology & medicine · 2023Article
- The role of selenoproteins in neurodevelopment and neurological function: Implications in autism spectrum disorder.Frontiers in molecular neuroscience · 2023Review
- Methionine oxidation activates pyruvate kinase M2 to promote pancreatic cancer metastasis.Molecular cell · 2022Article
- Selenophosphate synthetase 1 deficiency exacerbates osteoarthritis by dysregulating redox homeostasis.Nature communications · 2022Article
- Using selenocysteine-specific reporters to screen for efficient tRNAMethods in enzymology · 2022Article
61 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Methionine residues in proteins are susceptible to oxidation by reactive oxygen species, but can be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB). However, the identity of all methionine sulfoxide reductases involved, their cellular locations and relative contributions to the overall pathway are poorly understood. Here, we describe a methionine-R-sulfoxide reduction system in mammals, in which two MsrB homologues were previously described. We found that human and mouse genomes possess three MsrB genes and characterized their protein products, designated MsrB1, MsrB2, and MsrB3. MsrB1 (Selenoprotein R) was present in the cytosol and nucleus and exhibited the highest methionine-R-sulfoxide reductase activity because of the presence of selenocysteine (Sec) in its active site. Other mammalian MsrBs contained cysteine in place of Sec and were less catalytically efficient. MsrB2 (CBS-1) resided in mitochondria. It had high affinity for methionine-R-sulfoxide, but was inhibited by higher concentrations of the substrate. The human MsrB3 gene gave rise to two protein forms, MsrB3A and MsrB3B. These were generated by alternative splicing that introduced contrasting N-terminal and C-terminal signals, such that MsrB3A was targeted to the endoplasmic reticulum and MsrB3B to mitochondria. We found that only mitochondrial forms of mammalian MsrBs (MsrB2 and MsrB3B) could compensate for MsrA and MsrB deficiency in yeast. All mammalian MsrBs belonged to a group of zinc-containing proteins. The multiplicity of MsrBs contrasted with the presence of a single mammalian MsrA gene as well as with the occurrence of single MsrA and MsrB genes in yeast, fruit flies, and nematodes. The data suggested that different cellular compartments in mammals maintain a system for repair of oxidized methionine residues and that this function is tuned in enzyme- and stereo-specific manner.
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