The CHARGE syndrome-associated protein FAM172A controls AGO2 nuclear import
CHARGE syndrome is a neural crest-related disorder mainly caused by mutation of the chromatin remodeler-coding gene Alternative causes include mutation of other chromatin and/or splicing factors. One of these additional players is the poorly characterized FAM172A, which we previously found in a comp...
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| Veröffentlicht in: | Life science alliance 2023-08, Vol.6 (8), p.e202302133 |
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| creator | Sallis, Sephora Bérubé-Simard, Félix-Antoine Grondin, Benoit Leduc, Elizabeth Azouz, Fatiha Bélanger, Catherine Pilon, Nicolas |
| description | CHARGE syndrome is a neural crest-related disorder mainly caused by mutation of the chromatin remodeler-coding gene
Alternative causes include mutation of other chromatin and/or splicing factors. One of these additional players is the poorly characterized FAM172A, which we previously found in a complex with CHD7 and the small RNA-binding protein AGO2 at the chromatin-spliceosome interface. Focusing on the FAM172A-AGO2 interplay, we now report that FAM172A is a direct binding partner of AGO2 and, as such, one of the long sought-after regulators of AGO2 nuclear import. We show that this FAM172A function mainly relies on its classical bipartite nuclear localization signal and associated canonical importin-α/β pathway, being enhanced by CK2-induced phosphorylation and abrogated by a CHARGE syndrome-associated missense mutation. Overall, this study thus strengthens the notion that noncanonical nuclear functions of AGO2 and associated regulatory mechanisms might be clinically relevant. |
| doi_str_mv | 10.26508/lsa.202302133 |
| format | Article |
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Alternative causes include mutation of other chromatin and/or splicing factors. One of these additional players is the poorly characterized FAM172A, which we previously found in a complex with CHD7 and the small RNA-binding protein AGO2 at the chromatin-spliceosome interface. Focusing on the FAM172A-AGO2 interplay, we now report that FAM172A is a direct binding partner of AGO2 and, as such, one of the long sought-after regulators of AGO2 nuclear import. We show that this FAM172A function mainly relies on its classical bipartite nuclear localization signal and associated canonical importin-α/β pathway, being enhanced by CK2-induced phosphorylation and abrogated by a CHARGE syndrome-associated missense mutation. Overall, this study thus strengthens the notion that noncanonical nuclear functions of AGO2 and associated regulatory mechanisms might be clinically relevant.</description><identifier>ISSN: 2575-1077</identifier><identifier>EISSN: 2575-1077</identifier><identifier>DOI: 10.26508/lsa.202302133</identifier><identifier>PMID: 37221016</identifier><language>eng</language><publisher>United States: Life Science Alliance LLC</publisher><subject>Active Transport, Cell Nucleus ; CHARGE Syndrome ; Chromatin ; Humans ; Mutation, Missense ; Proteins</subject><ispartof>Life science alliance, 2023-08, Vol.6 (8), p.e202302133</ispartof><rights>2023 Sallis et al.</rights><rights>2023 Sallis et al. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-d369b6f97f1248d3337e06312e6cd98a8a80adda768100fc5f2cbcfcbde2364b3</citedby><cites>FETCH-LOGICAL-c391t-d369b6f97f1248d3337e06312e6cd98a8a80adda768100fc5f2cbcfcbde2364b3</cites><orcidid>0000-0003-3641-0776</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/PMC10205598/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10205598/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37221016$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sallis, Sephora</creatorcontrib><creatorcontrib>Bérubé-Simard, Félix-Antoine</creatorcontrib><creatorcontrib>Grondin, Benoit</creatorcontrib><creatorcontrib>Leduc, Elizabeth</creatorcontrib><creatorcontrib>Azouz, Fatiha</creatorcontrib><creatorcontrib>Bélanger, Catherine</creatorcontrib><creatorcontrib>Pilon, Nicolas</creatorcontrib><title>The CHARGE syndrome-associated protein FAM172A controls AGO2 nuclear import</title><title>Life science alliance</title><addtitle>Life Sci Alliance</addtitle><description>CHARGE syndrome is a neural crest-related disorder mainly caused by mutation of the chromatin remodeler-coding gene
Alternative causes include mutation of other chromatin and/or splicing factors. One of these additional players is the poorly characterized FAM172A, which we previously found in a complex with CHD7 and the small RNA-binding protein AGO2 at the chromatin-spliceosome interface. Focusing on the FAM172A-AGO2 interplay, we now report that FAM172A is a direct binding partner of AGO2 and, as such, one of the long sought-after regulators of AGO2 nuclear import. We show that this FAM172A function mainly relies on its classical bipartite nuclear localization signal and associated canonical importin-α/β pathway, being enhanced by CK2-induced phosphorylation and abrogated by a CHARGE syndrome-associated missense mutation. Overall, this study thus strengthens the notion that noncanonical nuclear functions of AGO2 and associated regulatory mechanisms might be clinically relevant.</description><subject>Active Transport, Cell Nucleus</subject><subject>CHARGE Syndrome</subject><subject>Chromatin</subject><subject>Humans</subject><subject>Mutation, Missense</subject><subject>Proteins</subject><issn>2575-1077</issn><issn>2575-1077</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUd9LwzAQDqK4Mffqo-TRl878aJv0ScpwmzgZyHwOaZK6StvUpBX23xvcHJM7uIP77ruP-wC4xWhG0gTxh9rLGUGEIoIpvQBjkrAkwoixy7N-BKbefyKESMg4ia_BiDJCMMLpGLxsdwbOV_nb8gn6faudbUwkvbeqkr3RsHO2N1ULF_krZiSHyra9s7WH-XJDYDuo2kgHq6azrr8BV6WsvZke6wS8L56281W03iyf5_k6UjTDfaRpmhVpmbESk5hrSikzKKWYmFTpjMsQSGotWcoxQqVKSqIKVapCG0LTuKAT8Hjg7YaiMVqZIEnWonNVI91eWFmJ_5O22okP-y1weEGSZDww3B8ZnP0ajO9FU3ll6lq2xg5eEI45izOOUIDODlDlrPfOlKc7GIlfF0RwQZxcCAt35-pO8L-f0x9zy4JC</recordid><startdate>20230801</startdate><enddate>20230801</enddate><creator>Sallis, Sephora</creator><creator>Bérubé-Simard, Félix-Antoine</creator><creator>Grondin, Benoit</creator><creator>Leduc, Elizabeth</creator><creator>Azouz, Fatiha</creator><creator>Bélanger, Catherine</creator><creator>Pilon, Nicolas</creator><general>Life Science Alliance LLC</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3641-0776</orcidid></search><sort><creationdate>20230801</creationdate><title>The CHARGE syndrome-associated protein FAM172A controls AGO2 nuclear import</title><author>Sallis, Sephora ; Bérubé-Simard, Félix-Antoine ; Grondin, Benoit ; Leduc, Elizabeth ; Azouz, Fatiha ; Bélanger, Catherine ; Pilon, Nicolas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-d369b6f97f1248d3337e06312e6cd98a8a80adda768100fc5f2cbcfcbde2364b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Active Transport, Cell Nucleus</topic><topic>CHARGE Syndrome</topic><topic>Chromatin</topic><topic>Humans</topic><topic>Mutation, Missense</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sallis, Sephora</creatorcontrib><creatorcontrib>Bérubé-Simard, Félix-Antoine</creatorcontrib><creatorcontrib>Grondin, Benoit</creatorcontrib><creatorcontrib>Leduc, Elizabeth</creatorcontrib><creatorcontrib>Azouz, Fatiha</creatorcontrib><creatorcontrib>Bélanger, Catherine</creatorcontrib><creatorcontrib>Pilon, Nicolas</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Life science alliance</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sallis, Sephora</au><au>Bérubé-Simard, Félix-Antoine</au><au>Grondin, Benoit</au><au>Leduc, Elizabeth</au><au>Azouz, Fatiha</au><au>Bélanger, Catherine</au><au>Pilon, Nicolas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The CHARGE syndrome-associated protein FAM172A controls AGO2 nuclear import</atitle><jtitle>Life science alliance</jtitle><addtitle>Life Sci Alliance</addtitle><date>2023-08-01</date><risdate>2023</risdate><volume>6</volume><issue>8</issue><spage>e202302133</spage><pages>e202302133-</pages><issn>2575-1077</issn><eissn>2575-1077</eissn><abstract>CHARGE syndrome is a neural crest-related disorder mainly caused by mutation of the chromatin remodeler-coding gene
Alternative causes include mutation of other chromatin and/or splicing factors. One of these additional players is the poorly characterized FAM172A, which we previously found in a complex with CHD7 and the small RNA-binding protein AGO2 at the chromatin-spliceosome interface. Focusing on the FAM172A-AGO2 interplay, we now report that FAM172A is a direct binding partner of AGO2 and, as such, one of the long sought-after regulators of AGO2 nuclear import. We show that this FAM172A function mainly relies on its classical bipartite nuclear localization signal and associated canonical importin-α/β pathway, being enhanced by CK2-induced phosphorylation and abrogated by a CHARGE syndrome-associated missense mutation. Overall, this study thus strengthens the notion that noncanonical nuclear functions of AGO2 and associated regulatory mechanisms might be clinically relevant.</abstract><cop>United States</cop><pub>Life Science Alliance LLC</pub><pmid>37221016</pmid><doi>10.26508/lsa.202302133</doi><orcidid>https://orcid.org/0000-0003-3641-0776</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Active Transport, Cell Nucleus CHARGE Syndrome Chromatin Humans Mutation, Missense Proteins |
| title | The CHARGE syndrome-associated protein FAM172A controls AGO2 nuclear import |
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