Sulfhydration mediates neuroprotective actions of parkin
Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s disease are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic Parkinson’s disease. Here we demonstrate that physiologic modi...
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| Veröffentlicht in: | Nature communications 2013-03, Vol.4 (1), p.1626-1626 |
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| creator | Vandiver, M. Scott Paul, Bindu D. Xu, Risheng Karuppagounder, Senthilkumar Rao, Feng Snowman, Adele M. Seok Ko, Han Il Lee, Yun Dawson, Valina L. Dawson, Ted M. Sen, Nilkantha Snyder, Solomon H. |
| description | Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s disease are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic Parkinson’s disease. Here we demonstrate that physiologic modification of parkin by hydrogen sulfide, termed sulfhydration, enhances its catalytic activity. Sulfhydration sites are identified by mass spectrometry analysis and are investigated by site-directed mutagenesis. Parkin sulfhydration is markedly depleted in the brains of patients with Parkinson’s disease, suggesting that this loss may be pathologic. This implies that hydrogen sulfide donors may be therapeutic.
The gasotransmitter hydrogen sulfide signals by sulfide modification of target proteins. Vandiver and colleagues study the sulfhydration of parkin by hydrogen sulfide and find that sulfhydration stimulates its activity, and that this activity is reduced in patients with Parkinson’s disease. |
| doi_str_mv | 10.1038/ncomms2623 |
| format | Article |
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The gasotransmitter hydrogen sulfide signals by sulfide modification of target proteins. Vandiver and colleagues study the sulfhydration of parkin by hydrogen sulfide and find that sulfhydration stimulates its activity, and that this activity is reduced in patients with Parkinson’s disease.</description><subject>631/378/1689/1718</subject><subject>631/378/340</subject><subject>692/308</subject><subject>Amino Acid Sequence</subject><subject>Catalysis</subject><subject>Humanities and Social Sciences</subject><subject>Hydrogen Sulfide - pharmacology</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Neuroprotective Agents - metabolism</subject><subject>Nitroso Compounds - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sulfhydryl Compounds - metabolism</subject><subject>Ubiquitin-Protein Ligases - chemistry</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitin-Protein Ligases - physiology</subject><issn>2041-1723</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpVkEtLAzEUhYMgttRu_AEy4FJGk9xMZrIRpPiCggt1HdI82qltMiYzhf57p7RqvZuzOIfvHg5CFwTfEAzVrddhvU6UUzhBQ4oZyUlJYYDGKS1xfyBIxdgZGlAooOCsHKLqrVu5xdZE1dbBZ2tratXalHnbxdDE0Frd1hubKb3zUxZc1qj4WftzdOrUKtnxQUfo4_HhffKcT1-fXib307yhtGzzCgMVqixsxYUgWmsgMMO0AC0wU8YoDRxKURlhXMW4ccwJZrgTXGHshIIRuttzm27Wt9PWt1GtZBPrtYpbGVQt_zu-Xsh52EjglApW9ICrAyCGr86mVi5DF33fWRKghFCKK9qnLo_f_PJ_luoD1_tA6i0_t_EIg-Vufvk3P3wD8Bd5bQ</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>Vandiver, M. 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Scott</au><au>Paul, Bindu D.</au><au>Xu, Risheng</au><au>Karuppagounder, Senthilkumar</au><au>Rao, Feng</au><au>Snowman, Adele M.</au><au>Seok Ko, Han</au><au>Il Lee, Yun</au><au>Dawson, Valina L.</au><au>Dawson, Ted M.</au><au>Sen, Nilkantha</au><au>Snyder, Solomon H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sulfhydration mediates neuroprotective actions of parkin</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2013-03-01</date><risdate>2013</risdate><volume>4</volume><issue>1</issue><spage>1626</spage><epage>1626</epage><pages>1626-1626</pages><eissn>2041-1723</eissn><abstract>Increases in S-nitrosylation and inactivation of the neuroprotective ubiquitin E3 ligase, parkin, in the brains of patients with Parkinson’s disease are thought to be pathogenic and suggest a possible mechanism linking parkin to sporadic Parkinson’s disease. Here we demonstrate that physiologic modification of parkin by hydrogen sulfide, termed sulfhydration, enhances its catalytic activity. Sulfhydration sites are identified by mass spectrometry analysis and are investigated by site-directed mutagenesis. Parkin sulfhydration is markedly depleted in the brains of patients with Parkinson’s disease, suggesting that this loss may be pathologic. This implies that hydrogen sulfide donors may be therapeutic.
The gasotransmitter hydrogen sulfide signals by sulfide modification of target proteins. Vandiver and colleagues study the sulfhydration of parkin by hydrogen sulfide and find that sulfhydration stimulates its activity, and that this activity is reduced in patients with Parkinson’s disease.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23535647</pmid><doi>10.1038/ncomms2623</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/378/1689/1718 631/378/340 692/308 Amino Acid Sequence Catalysis Humanities and Social Sciences Hydrogen Sulfide - pharmacology Mass Spectrometry Molecular Sequence Data multidisciplinary Neuroprotective Agents - metabolism Nitroso Compounds - metabolism Science Science (multidisciplinary) Sulfhydryl Compounds - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism Ubiquitin-Protein Ligases - physiology |
| title | Sulfhydration mediates neuroprotective actions of parkin |
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