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S-guanylation proteomics for redox-based mitochondrial signaling.
Md Mizanur Rahaman1, Tomohiro Sawa, Ahmed Khandaker Ahtesham
11 Department of Microbiology, Graduate School of Medical Sciences, Kumamoto University , Kumamoto, Japan .
Antioxidants & Redox Signaling
|September 18, 2012
Summary
8-nitroguanosine 3
Area of Science:
- Mitochondrial redox signaling
- Post-translational modifications
- Proteomics
Background:
- 8-nitroguanosine 3',5'-cyclic monophosphate (8-Nitro-cGMP) acts as an electrophilic second messenger.
- 8-Nitro-cGMP regulates redox signaling through protein S-guanylation.
- Mitochondrial reactive oxygen species contribute to 8-Nitro-cGMP formation.
Purpose of the Study:
- Investigate endogenous mitochondrial protein S-guanylation using S-guanylation proteomics.
- Identify novel mitochondrial targets of protein S-guanylation.
- Elucidate the role of S-guanylation in mitochondrial function and redox signaling.
Main Methods:
- Developed a mass spectrometry-based S-guanylation proteomics method.
- Employed direct protein digestion with immunoaffinity capture and LC-MS/MS.
- Utilized 2D-gel electrophoresis followed by in-gel digestion and LC-MS/MS.
Main Results:
- Identified endogenous S-guanylated mitochondrial proteins, including mortalin and HSP60.
- Mortalin and HSP60 are implicated in regulating mitochondrial permeability-transition pore (mPTP) opening.
- Immunological stimulation and 8-Nitro-cGMP induced mPTP opening in a cyclophilin D-dependent manner.
Conclusions:
- Mitochondrial heat-shock proteins (HSPs) are novel targets for redox modification via S-guanylation.
- Protein S-guanylation plays a role in mPTP regulation.
- S-guanylation contributes to mitochondrial redox signaling pathways.
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