α-Synuclein reduces acetylserotonin O-methyltransferase mediated melatonin biosynthesis by microtubule-associated protein 1 light chain 3 beta-related degradation pathway
Previous studies have demonstrated that α-synuclein (α-SYN) is closely associated with rapid eye movement sleep behavior disorder (RBD) related to several neurodegenerative disorders. However, the exact molecular mechanisms are still rarely investigated. In the present study, we found that in the α-...
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| creator | Jia, Congcong Tian, Lulu Cheng, Cheng Zhang, Jun Al-Nusaif, Murad Li, Tianbai Yang, Huijia Lin, Yushan Li, Song Le, Weidong |
| description | Previous studies have demonstrated that α-synuclein (α-SYN) is closely associated with rapid eye movement sleep behavior disorder (RBD) related to several neurodegenerative disorders. However, the exact molecular mechanisms are still rarely investigated. In the present study, we found that in the α-SYN
A53T
induced RBD-like behavior mouse model, the melatonin level in the plasma and pineal gland were significantly decreased. To elucidate the underlying mechanism of α-SYN-induced melatonin reduction, we investigated the effect of α-SYN in melatonin biosynthesis. Our findings showed that α-SYN reduced the level and activity of melatonin synthesis enzyme acetylserotonin O-methyltransferase (ASMT) in the pineal gland and in the cell cultures. In addition, we found that microtubule-associated protein 1 light chain 3 beta (LC3B) as an important autophagy adapter is involved in the degradation of ASMT. Immunoprecipitation assays revealed that α-SYN increases the binding between LC3B and ASMT, leading to ASMT degradation and a consequent reduction in melatonin biosynthesis. Collectively, our results demonstrate the molecular mechanisms of α-SYN in melatonin biosynthesis, indicating that melatonin is an important molecule involved in the α-SYN-associated RBD-like behaviors, which may provide a potential therapeutic target for RBD of Parkinson’s disease. |
| doi_str_mv | 10.1007/s00018-023-05053-7 |
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A53T
induced RBD-like behavior mouse model, the melatonin level in the plasma and pineal gland were significantly decreased. To elucidate the underlying mechanism of α-SYN-induced melatonin reduction, we investigated the effect of α-SYN in melatonin biosynthesis. Our findings showed that α-SYN reduced the level and activity of melatonin synthesis enzyme acetylserotonin O-methyltransferase (ASMT) in the pineal gland and in the cell cultures. In addition, we found that microtubule-associated protein 1 light chain 3 beta (LC3B) as an important autophagy adapter is involved in the degradation of ASMT. Immunoprecipitation assays revealed that α-SYN increases the binding between LC3B and ASMT, leading to ASMT degradation and a consequent reduction in melatonin biosynthesis. Collectively, our results demonstrate the molecular mechanisms of α-SYN in melatonin biosynthesis, indicating that melatonin is an important molecule involved in the α-SYN-associated RBD-like behaviors, which may provide a potential therapeutic target for RBD of Parkinson’s disease.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-023-05053-7</identifier><identifier>PMID: 38279053</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Acetylserotonin O-Methyltransferase - chemistry ; Acetylserotonin O-Methyltransferase - metabolism ; alpha-Synuclein - metabolism ; Animals ; Autophagy ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Biosynthesis ; Cell Biology ; Degradation ; Endocrine system ; Immunoprecipitation ; Life Sciences ; Melatonin ; Melatonin - metabolism ; Methyltransferase ; Mice ; Microtubule-associated protein 1 ; Molecular modelling ; Movement disorders ; Neurodegenerative diseases ; Original ; Original Article ; Parkinson's disease ; Photodegradation ; Pineal gland ; Pineal Gland - metabolism ; Protein biosynthesis ; Proteins ; Reduction ; REM sleep ; Sleep disorders ; Synuclein ; Therapeutic targets</subject><ispartof>Cellular and molecular life sciences : CMLS, 2024-12, Vol.81 (1), p.61-61, Article 61</ispartof><rights>The Author(s), under exclusive licence to Springer Nature Switzerland AG 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c426t-c46673e2e1ecff7df3aa8e081695f809500c54ad2b4d9669a6ea4b2d8f1c46d33</cites><orcidid>0000-0001-7459-2705</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11072826/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11072826/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41120,41488,42189,42557,51319,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1007/s00018-023-05053-7$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38279053$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jia, Congcong</creatorcontrib><creatorcontrib>Tian, Lulu</creatorcontrib><creatorcontrib>Cheng, Cheng</creatorcontrib><creatorcontrib>Zhang, Jun</creatorcontrib><creatorcontrib>Al-Nusaif, Murad</creatorcontrib><creatorcontrib>Li, Tianbai</creatorcontrib><creatorcontrib>Yang, Huijia</creatorcontrib><creatorcontrib>Lin, Yushan</creatorcontrib><creatorcontrib>Li, Song</creatorcontrib><creatorcontrib>Le, Weidong</creatorcontrib><title>α-Synuclein reduces acetylserotonin O-methyltransferase mediated melatonin biosynthesis by microtubule-associated protein 1 light chain 3 beta-related degradation pathway</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Previous studies have demonstrated that α-synuclein (α-SYN) is closely associated with rapid eye movement sleep behavior disorder (RBD) related to several neurodegenerative disorders. However, the exact molecular mechanisms are still rarely investigated. In the present study, we found that in the α-SYN
A53T
induced RBD-like behavior mouse model, the melatonin level in the plasma and pineal gland were significantly decreased. To elucidate the underlying mechanism of α-SYN-induced melatonin reduction, we investigated the effect of α-SYN in melatonin biosynthesis. Our findings showed that α-SYN reduced the level and activity of melatonin synthesis enzyme acetylserotonin O-methyltransferase (ASMT) in the pineal gland and in the cell cultures. In addition, we found that microtubule-associated protein 1 light chain 3 beta (LC3B) as an important autophagy adapter is involved in the degradation of ASMT. Immunoprecipitation assays revealed that α-SYN increases the binding between LC3B and ASMT, leading to ASMT degradation and a consequent reduction in melatonin biosynthesis. Collectively, our results demonstrate the molecular mechanisms of α-SYN in melatonin biosynthesis, indicating that melatonin is an important molecule involved in the α-SYN-associated RBD-like behaviors, which may provide a potential therapeutic target for RBD of Parkinson’s disease.</description><subject>Acetylserotonin O-Methyltransferase - chemistry</subject><subject>Acetylserotonin O-Methyltransferase - metabolism</subject><subject>alpha-Synuclein - metabolism</subject><subject>Animals</subject><subject>Autophagy</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Biosynthesis</subject><subject>Cell Biology</subject><subject>Degradation</subject><subject>Endocrine system</subject><subject>Immunoprecipitation</subject><subject>Life Sciences</subject><subject>Melatonin</subject><subject>Melatonin - metabolism</subject><subject>Methyltransferase</subject><subject>Mice</subject><subject>Microtubule-associated protein 1</subject><subject>Molecular modelling</subject><subject>Movement disorders</subject><subject>Neurodegenerative diseases</subject><subject>Original</subject><subject>Original Article</subject><subject>Parkinson's disease</subject><subject>Photodegradation</subject><subject>Pineal gland</subject><subject>Pineal Gland - metabolism</subject><subject>Protein biosynthesis</subject><subject>Proteins</subject><subject>Reduction</subject><subject>REM sleep</subject><subject>Sleep disorders</subject><subject>Synuclein</subject><subject>Therapeutic targets</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kstu1TAQhiMEoqXwAixQJDZsDLZzcbxCqOImVeoCkNhZE2dy4ipxDrYDyjN11RfhmZhDDuWyYOPL-Pt_e8aTZY8Ffy44Vy8i51w0jMuC8YpXBVN3slNRSs40V-LucV038vNJ9iDGK6KrRtb3s5OikUqT4jS7_n7DPqx-sSM6nwfsFosxB4tpHSOGOc2e4pdswjSsYwrgY48BIuYTdg4SdrQYYcNaN8fVpwGji3m75pOz5LC0y4gMYpztJthT8HCbyEe3G1JuB6BdkbeYgIWDG0Ed7gJ0kNzs8z2k4RusD7N7PdCrHh3ns-zTm9cfz9-xi8u3789fXTBbyjrRWNeqQIkCbd-rri8AGuSNqHXVN1xXnNuqhE62ZafrWkONULaya3pB0q4ozrKXm-9-aSlLi57yHs0-uAnCamZw5u8T7wazm78aIbiSVGFyeHZ0CPOXBWMyk4sWxxE8zks0UgutCq11Q-jTf9CreQme8jtQjaqVlpIouVFU0BgD9revEdwcmsFszWCoGczPZjCKRE_-zONW8uv3CSg2INKR32H4ffd_bH8AS7LGnA</recordid><startdate>20241201</startdate><enddate>20241201</enddate><creator>Jia, Congcong</creator><creator>Tian, Lulu</creator><creator>Cheng, Cheng</creator><creator>Zhang, Jun</creator><creator>Al-Nusaif, Murad</creator><creator>Li, Tianbai</creator><creator>Yang, Huijia</creator><creator>Lin, Yushan</creator><creator>Li, Song</creator><creator>Le, Weidong</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-7459-2705</orcidid></search><sort><creationdate>20241201</creationdate><title>α-Synuclein reduces acetylserotonin O-methyltransferase mediated melatonin biosynthesis by microtubule-associated protein 1 light chain 3 beta-related degradation pathway</title><author>Jia, Congcong ; 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A53T
induced RBD-like behavior mouse model, the melatonin level in the plasma and pineal gland were significantly decreased. To elucidate the underlying mechanism of α-SYN-induced melatonin reduction, we investigated the effect of α-SYN in melatonin biosynthesis. Our findings showed that α-SYN reduced the level and activity of melatonin synthesis enzyme acetylserotonin O-methyltransferase (ASMT) in the pineal gland and in the cell cultures. In addition, we found that microtubule-associated protein 1 light chain 3 beta (LC3B) as an important autophagy adapter is involved in the degradation of ASMT. Immunoprecipitation assays revealed that α-SYN increases the binding between LC3B and ASMT, leading to ASMT degradation and a consequent reduction in melatonin biosynthesis. Collectively, our results demonstrate the molecular mechanisms of α-SYN in melatonin biosynthesis, indicating that melatonin is an important molecule involved in the α-SYN-associated RBD-like behaviors, which may provide a potential therapeutic target for RBD of Parkinson’s disease.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>38279053</pmid><doi>10.1007/s00018-023-05053-7</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-7459-2705</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylserotonin O-Methyltransferase - chemistry Acetylserotonin O-Methyltransferase - metabolism alpha-Synuclein - metabolism Animals Autophagy Biochemistry Biomedical and Life Sciences Biomedicine Biosynthesis Cell Biology Degradation Endocrine system Immunoprecipitation Life Sciences Melatonin Melatonin - metabolism Methyltransferase Mice Microtubule-associated protein 1 Molecular modelling Movement disorders Neurodegenerative diseases Original Original Article Parkinson's disease Photodegradation Pineal gland Pineal Gland - metabolism Protein biosynthesis Proteins Reduction REM sleep Sleep disorders Synuclein Therapeutic targets |
| title | α-Synuclein reduces acetylserotonin O-methyltransferase mediated melatonin biosynthesis by microtubule-associated protein 1 light chain 3 beta-related degradation pathway |
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