التفاصيل البيبلوغرافية
| العنوان: |
Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1 |
| المؤلفون: |
Aracena Parks, Paula, Goonasekera, Sanjeewa A., Gilman, Charles P., Dirksen, Robert T., Hidalgo, Cecilia, Hamilton, Susan L. |
| بيانات النشر: |
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| سنة النشر: |
2006 |
| المجموعة: |
Universidad de Chile: Captura |
| مصطلحات موضوعية: |
CA2+ RELEASE CHANNEL, MUSCLE SARCOPLASMIC-RETICULUM, CENTRAL CORE DISEASE, CALCIUM-RELEASE, MALIGNANT HYPERTHERMIA, NITRIC-OXIDE, CALMODULIN-BINDING, FKBP12 BINDING, REDOX SENSOR, SKELETAL |
| الوصف: |
The skeletal muscle Ca2+-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, H2O2 treatment of C3635A-RyR1 channels or wildtype RyR1, following their expression in human embryonic kidney cells, enhances [H-3] 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 isotope-coded 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). |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| تدمد: |
0021-9258 |
| العلاقة: |
JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 281 Issue: 52 Pages: 40354-40368 Published: DEC 29 2006; http://www.captura.uchile.cl/handle/2250/5379Test |
| الإتاحة: |
http://www.captura.uchile.cl/handle/2250/5379Test |
| رقم الانضمام: |
edsbas.E57B33B4 |
| قاعدة البيانات: |
BASE |
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