Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases
In this News and Views, I discuss our recent publication that established how steroidogenic acute regulatory-related lipid transfer domain-3 (STARD3), a membrane contact protein situated at lysosomal membranes, plays a role in the detoxification of cholesterol hydroperoxide. STARD3's methionine...
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| Format: | Article |
| Language: | English |
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SAGE Publishing
2024-01-01
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| Series: | Contact |
| Online Access: | https://doi.org/10.1177/25152564231223480 |
| _version_ | 1797366148524670976 |
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| author | Jung Mi Lim |
| author_facet | Jung Mi Lim |
| author_sort | Jung Mi Lim |
| collection | DOAJ |
| description | In this News and Views, I discuss our recent publication that established how steroidogenic acute regulatory-related lipid transfer domain-3 (STARD3), a membrane contact protein situated at lysosomal membranes, plays a role in the detoxification of cholesterol hydroperoxide. STARD3's methionine residues can be oxidized to methionine sulfoxide by cholesterol hydroperoxide, after which methionine sulfoxide reductases reduce the methionine sulfoxide residues back to methionine. The reaction also results in the reduction of the cholesterol hydroperoxide to an alcohol. The cyclic oxidation and reduction of methionine residues in STARD3 at membrane contact sites creates a catalytically efficient mechanism for detoxification of cholesterol hydroperoxide during cholesterol transport, thus protecting membrane contact sites and the entire cell against the toxicity of cholesterol hydroperoxide. |
| first_indexed | 2024-03-08T17:00:11Z |
| format | Article |
| id | doaj.art-b81512ec390e460f8c8b59ccc1dc8e73 |
| institution | Directory Open Access Journal |
| issn | 2515-2564 |
| language | English |
| last_indexed | 2024-03-08T17:00:11Z |
| publishDate | 2024-01-01 |
| publisher | SAGE Publishing |
| record_format | Article |
| series | Contact |
| spelling | doaj.art-b81512ec390e460f8c8b59ccc1dc8e732024-01-04T15:03:22ZengSAGE PublishingContact2515-25642024-01-01710.1177/25152564231223480Protection of Membrane Contact Protein by the Methionine Sulfoxide ReductasesJung Mi LimIn this News and Views, I discuss our recent publication that established how steroidogenic acute regulatory-related lipid transfer domain-3 (STARD3), a membrane contact protein situated at lysosomal membranes, plays a role in the detoxification of cholesterol hydroperoxide. STARD3's methionine residues can be oxidized to methionine sulfoxide by cholesterol hydroperoxide, after which methionine sulfoxide reductases reduce the methionine sulfoxide residues back to methionine. The reaction also results in the reduction of the cholesterol hydroperoxide to an alcohol. The cyclic oxidation and reduction of methionine residues in STARD3 at membrane contact sites creates a catalytically efficient mechanism for detoxification of cholesterol hydroperoxide during cholesterol transport, thus protecting membrane contact sites and the entire cell against the toxicity of cholesterol hydroperoxide.https://doi.org/10.1177/25152564231223480 |
| spellingShingle | Jung Mi Lim Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases Contact |
| title | Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases |
| title_full | Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases |
| title_fullStr | Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases |
| title_full_unstemmed | Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases |
| title_short | Protection of Membrane Contact Protein by the Methionine Sulfoxide Reductases |
| title_sort | protection of membrane contact protein by the methionine sulfoxide reductases |
| url | https://doi.org/10.1177/25152564231223480 |
| work_keys_str_mv | AT jungmilim protectionofmembranecontactproteinbythemethioninesulfoxidereductases |