ArticleBiophysical journal2001
Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 49 citations in OpenAlex.
- Misfolded protein oligomers induce an increase of intracellular CaCellular and molecular life sciences : CMLS · 2022Article
- The calmodulin redox sensor controls myogenesis.PloS one · 2020Article
- Oxidative stress and phosphatidylserine exposure in red cells from patients with sickle cell anaemia.British journal of haematology · 2018Article
- 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
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding.The Journal of biological chemistry · 2012Article
- An altered mode of calcium coordination in methionine-oxidized calmodulin.Biophysical journal · 2008Article
- Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensis.Biochemistry · 2007Article
- Oxidation of calmodulin alters activation and regulation of CaMKII.Biochemical and biophysical research communications · 2007Article
- Mechanism of calmodulin recognition of the binding domain of isoform 1b of the plasma membrane Ca(2+)-ATPase: kinetic pathway and effects of methionine oxidation.Biochemistry · 2007Article
- Calmodulin, conformational states, and calcium signaling. A single-molecule perspective.Biochemistry · 2006Article
- Tertiary structural rearrangements upon oxidation of Methionine145 in calmodulin promotes targeted proteasomal degradation.Biophysical journal · 2006Article
- Rapid method for quantifying the extent of methionine oxidation in intact calmodulin.Journal of the American Society for Mass Spectrometry · 2005Article
- Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Oxidation of either Met(145) or Met(146) in wheat germ calmodulin (CaM) to methionine sulfoxide prevents the CaM-dependent activation of the plasma membrane (PM) Ca-ATPase (D. Yin, K. Kuczera, and T. C. Squier, 2000, Chem. Res. Toxicol. 13:103-110). To investigate the structural basis for the inhibition of the PM-Ca-ATPase by oxidized CaM (CaM(ox)), we have used circular dichroism (CD) and fluorescence spectroscopy to resolve conformational differences within the complex between CaM and the PM-Ca-ATPase. The similar excited-state lifetime and solvent accessibility of the fluorophore N-1-pyrenyl-maleimide covalently bound to Cys(26) in unoxidized CaM and CaM(ox) indicates that the globular domains within CaM(ox) assume a native-like structure following association with the PM-Ca-ATPase. However, in comparison with oxidized CaM there are increases in the 1) molar ellipticity in the CD spectrum and 2) conformational heterogeneity between the opposing globular domains for CaM(ox) bound to the CaM-binding sequence of the PM-Ca-ATPase. Furthermore, CaM(ox) binds to the PM-Ca-ATPase with high affinity at a distinct, but overlapping, site to that normally occupied by unoxidized CaM. These results suggest that alterations in binding interactions between CaM(ox) and the PM-Ca-ATPase block important structural transitions within the CaM-binding sequence of the PM-Ca-ATPase that are normally associated with enzyme activation.
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