Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1.

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Abstract Text:

Paula Aracena-Parks,Sanjeewa A Goonasekera,Charles P Gilman,Robert T Dirksen,Cecilia Hidalgo,Susan L Hamilton,

The skeletal muscle Ca(2+)-release channel (ryanodine receptor type 1 (RyR1)) is a redox sensor, susceptible to reversible S-nitrosylation, S-glutathionylation, and disulfide oxidation. So far, Cys-3635 remains the only cysteine residue identified as functionally relevant to the redox sensing properties of the channel. We demonstrate that expression of the C3635A-RyR1 mutant in RyR1-null myotubes alters the sensitivity of the ryanodine receptor to activation by voltage, indicating that Cys-3635 is involved in voltage-gated excitation-contraction coupling. However, H(2)O(2) treatment of C3635A-RyR1 channels or wild-type RyR1, following their expression in human embryonic kidney cells, enhances [(3)H]ryanodine binding to the same extent, suggesting that cysteines other than Cys-3635 are responsible for the oxidative enhancement of channel activity. Using a combination of Western blotting and sulfhydryl-directed fluorescent labeling, we found that two large regions of RyR1 (amino acids 1-2401 and 3120-4475), previously shown to be involved in disulfide bond formation, are also major sites of both S-nitrosylation and S-glutathionylation. Using selective isotopecoded affinity tag labeling of RyR1 and matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy, we identified, out of the 100 cysteines in each RyR1 subunit, 9 that are endogenously modified (Cys-36, Cys-315, Cys-811, Cys-906, Cys-1591, Cys-2326, Cys-2363, Cys-3193, and Cys-3635) and another 3 residues that were only modified with exogenous redox agents (Cys-253, Cys-1040, and Cys-1303). We also identified the types of redox modification each of these cysteines can undergo. In summary, we have identified a discrete subset of cysteines that are likely to be involved in the functional response of RyR1 to different redox modifications (S-nitrosylation, S-glutathionylation, and oxidation to disulfides).

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Publishing Authors By Initials

P Aracena-Parks,SA Goonasekera,CP Gilman,RT Dirksen,C Hidalgo,SL Hamilton,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

PUBMED ID PMID:

MEDLINE DATE:

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 40354-68

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 27

MONTH: 10

YEAR: 2006

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: metabolism

Chemical & Substance for Abstract: Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1.

AFFILIATION: Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas 77030, USA.

Country: United States

AGENCY: United States NIAMS

GRANT: AR44657

ACRONYM: AR

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1 Related Publications

• 'Physical Inactivity' (Low NEAT) is NOT the Same Physiologically as the 'Lack of Exercise'?: 342: 1:05 PM -1:15 PM.
• Analysis of association between the serotonin transporter and antidepressant response in a large clinical sample.
• Are Chemical (Lipase Dependent) Signals Sufficient to Mimic Exercise-Induced Endothelial Phenotypes?: 67: 1:35 PM-2:00 PM.
• Arsenic disruption of steroid receptor gene activation: Complex dose-response effects are shared by several steroid receptors.
• Associations of Ki-ras proto-oncogene mutation and p53 gene overexpression in sporadic colorectal adenomas with demographic and clinicopathologic characteristics.
• Automated Quantification of Lymph Node Size and Number in Surgical Specimens of Stage II Colorectal Cancer.
• Developing clinical standards and accrediting clinics in infertility care.
• Diphenylindane-based proteomimetics reproduce the projection of the i, i+3, i+4, and i+7 residues on an alpha-helix.
• Effects of eccentric contractions on skeletal muscle function in a malignant hyperthermia mouse model: 2352: board #31 june 1 2:00 PM -3:30 PM.
• Fibroblast growth factor causes an early increase in phosphorylation of a membrane protein in quiescent 3T3 cells.
• Gene-lifecourse interaction for alcohol consumption in adolescence and young adulthood: five monoamine genes.
• Helix mimetics as inhibitors of the interaction of the estrogen receptor with coactivator peptides.
• Identification of atherosclerotic lipid deposits by diffusion-weighted imaging.
• Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1.
• Introduction and Overview: 341: 1:00 PM-1:05 PM.
• Introduction and Overview: 65: 1:00 PM-1:10 PM.
• Modifications of the GSK3beta substrate sequence to produce substrate-mimetic inhibitors of Akt as potential anti-cancer therapeutics.
• Nonlinear surface waves in soft, weakly compressible elastic media.
• Prize-based contingency management does not increase gambling.
• Protein-protein interaction inhibitors: small molecules from screening techniques.
• Recognition of solvent exposed protein surfaces using anthracene derived receptors.
• Shifts in thioredoxin reductase activity and oxidant status in mononuclear cells obtained from transition dairy cattle.
• Signaling in lipopolysaccharide-induced stabilization of formyl peptide receptor 1 mRNA in mouse peritoneal macrophages.
• Sociology-the poor relation in alcohol and drug research?
• Sonotubometry.
• Structure-activity studies on a library of potent calix[4]arene-based PDGF antagonists that inhibit PDGF-stimulated PDGFR tyrosine phosphorylation.
• Synthesis and evaluation of potent, highly-selective, 3-aryl-piperazinone inhibitors of protein geranylgeranyltransferase-I.
• Synthetic non-peptide mimetics of alpha-helices.
• Two lyophilized polymer matrix recombinant human bone morphogenetic protein-2 carriers in rabbit calvarial defects.
• Zfp423 controls proliferation and differentiation of neural precursors in cerebellar vermis formation.