Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes
Chromatin disorganization is one of the major alterations linked to prelamin A processing impairment. In this study we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure. We show that when prelamin A and BAF cannot properly interact no prelamin A-dependent effect...
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| Veröffentlicht in: | Oncotarget 2016-03, Vol.7 (13), p.15662-15677 |
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| creator | Loi, Manuela Cenni, Vittoria Duchi, Serena Squarzoni, Stefano Lopez-Otin, Carlos Foisner, Roland Lattanzi, Giovanna Capanni, Cristina |
| description | Chromatin disorganization is one of the major alterations linked to prelamin A processing impairment. In this study we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure. We show that when prelamin A and BAF cannot properly interact no prelamin A-dependent effects on chromatin occur; similar to what is observed in human Nestor Guillermo Progeria Syndrome cells harboring a BAF mutation, in HEK293 cells expressing a BAF mutant unable to bind prelamin A, or in siRNA mediated BAF-depleted HEK293 cells expressing prelamin A. BAF is necessary to induce histone trimethyl-H3K9 as well as HP1-alpha and LAP2-alpha nuclear relocalization in response to prelamin A accumulation. These findings are enforced by electron microscopy evaluations showing how the prelamin A-BAF interaction governs overall chromatin organization. Finally, we demonstrate that the LAP2-alpha nuclear localization defect observed in HGPS cells involves the progerin-BAF interaction, thus establishing a functional link between BAF and prelamin A pathological forms. |
| doi_str_mv | 10.18632/oncotarget.6697 |
| format | Article |
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In this study we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure. We show that when prelamin A and BAF cannot properly interact no prelamin A-dependent effects on chromatin occur; similar to what is observed in human Nestor Guillermo Progeria Syndrome cells harboring a BAF mutation, in HEK293 cells expressing a BAF mutant unable to bind prelamin A, or in siRNA mediated BAF-depleted HEK293 cells expressing prelamin A. BAF is necessary to induce histone trimethyl-H3K9 as well as HP1-alpha and LAP2-alpha nuclear relocalization in response to prelamin A accumulation. These findings are enforced by electron microscopy evaluations showing how the prelamin A-BAF interaction governs overall chromatin organization. Finally, we demonstrate that the LAP2-alpha nuclear localization defect observed in HGPS cells involves the progerin-BAF interaction, thus establishing a functional link between BAF and prelamin A pathological forms.</description><identifier>ISSN: 1949-2553</identifier><identifier>EISSN: 1949-2553</identifier><identifier>DOI: 10.18632/oncotarget.6697</identifier><identifier>PMID: 26701887</identifier><language>eng</language><publisher>United States: Impact Journals LLC</publisher><subject>Chromatin - metabolism ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; HEK293 Cells ; Humans ; Lamin Type A - metabolism ; Mutation ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Progeria - genetics ; Progeria - metabolism ; Progeria - pathology ; Research Paper</subject><ispartof>Oncotarget, 2016-03, Vol.7 (13), p.15662-15677</ispartof><rights>Copyright: © 2016 Loi et al. 2016</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-25b713b6e5fe764ea4f0ce7a71fdec842819a3b5b207b3abbb318787c2f92bfa3</citedby><cites>FETCH-LOGICAL-c354t-25b713b6e5fe764ea4f0ce7a71fdec842819a3b5b207b3abbb318787c2f92bfa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941268/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941268/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26701887$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Loi, Manuela</creatorcontrib><creatorcontrib>Cenni, Vittoria</creatorcontrib><creatorcontrib>Duchi, Serena</creatorcontrib><creatorcontrib>Squarzoni, Stefano</creatorcontrib><creatorcontrib>Lopez-Otin, Carlos</creatorcontrib><creatorcontrib>Foisner, Roland</creatorcontrib><creatorcontrib>Lattanzi, Giovanna</creatorcontrib><creatorcontrib>Capanni, Cristina</creatorcontrib><title>Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes</title><title>Oncotarget</title><addtitle>Oncotarget</addtitle><description>Chromatin disorganization is one of the major alterations linked to prelamin A processing impairment. In this study we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure. We show that when prelamin A and BAF cannot properly interact no prelamin A-dependent effects on chromatin occur; similar to what is observed in human Nestor Guillermo Progeria Syndrome cells harboring a BAF mutation, in HEK293 cells expressing a BAF mutant unable to bind prelamin A, or in siRNA mediated BAF-depleted HEK293 cells expressing prelamin A. BAF is necessary to induce histone trimethyl-H3K9 as well as HP1-alpha and LAP2-alpha nuclear relocalization in response to prelamin A accumulation. These findings are enforced by electron microscopy evaluations showing how the prelamin A-BAF interaction governs overall chromatin organization. Finally, we demonstrate that the LAP2-alpha nuclear localization defect observed in HGPS cells involves the progerin-BAF interaction, thus establishing a functional link between BAF and prelamin A pathological forms.</description><subject>Chromatin - metabolism</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Lamin Type A - metabolism</subject><subject>Mutation</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Progeria - genetics</subject><subject>Progeria - metabolism</subject><subject>Progeria - pathology</subject><subject>Research Paper</subject><issn>1949-2553</issn><issn>1949-2553</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUcFqGzEUFCWhNqnvPZU9JodNV9LuSnsp2CFJC4Fe0rN4kt-uFXYlV5IN7ddHjtPEfZc38GbmDQwhn2l1TWXL2VfvjE8QBkzXbduJD2ROu7orWdPwsxM8I4sYn6o8TS0k6z6SGWtFRaUUc7JZQQgWQ5l8CbvkrUs4BEjWu6IHk3woLlfLu6vCur0f9zihSxkX24AjTBksywNKuC7MJvgpK13hwwDO_j26mA24AeMnct7DGHHxui_Ir7vbx5vv5cPP-x83y4fS8KZOObAWlOsWmx5FWyPUfWVQgKD9Go2smaQdcN1oVgnNQWvNqRRSGNZ3TPfAL8i3o-92pydcm5w3wKi2wU4Q_igPVv1_cXajBr9XdVdT1spscPlqEPzvHcakJhsNjiM49LuoqOgoZy2taKZWR6oJPsaA_dsbWqmXjtR7R-rQUZZ8OY33JvjXCH8GKpmTcw</recordid><startdate>20160329</startdate><enddate>20160329</enddate><creator>Loi, Manuela</creator><creator>Cenni, Vittoria</creator><creator>Duchi, Serena</creator><creator>Squarzoni, Stefano</creator><creator>Lopez-Otin, Carlos</creator><creator>Foisner, Roland</creator><creator>Lattanzi, Giovanna</creator><creator>Capanni, Cristina</creator><general>Impact Journals 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></search><sort><creationdate>20160329</creationdate><title>Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes</title><author>Loi, Manuela ; Cenni, Vittoria ; Duchi, Serena ; Squarzoni, Stefano ; Lopez-Otin, Carlos ; Foisner, Roland ; Lattanzi, Giovanna ; Capanni, Cristina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-25b713b6e5fe764ea4f0ce7a71fdec842819a3b5b207b3abbb318787c2f92bfa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Chromatin - metabolism</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Lamin Type A - metabolism</topic><topic>Mutation</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Progeria - genetics</topic><topic>Progeria - metabolism</topic><topic>Progeria - pathology</topic><topic>Research Paper</topic><toplevel>online_resources</toplevel><creatorcontrib>Loi, Manuela</creatorcontrib><creatorcontrib>Cenni, Vittoria</creatorcontrib><creatorcontrib>Duchi, Serena</creatorcontrib><creatorcontrib>Squarzoni, Stefano</creatorcontrib><creatorcontrib>Lopez-Otin, Carlos</creatorcontrib><creatorcontrib>Foisner, Roland</creatorcontrib><creatorcontrib>Lattanzi, Giovanna</creatorcontrib><creatorcontrib>Capanni, Cristina</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>Oncotarget</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Loi, Manuela</au><au>Cenni, Vittoria</au><au>Duchi, Serena</au><au>Squarzoni, Stefano</au><au>Lopez-Otin, Carlos</au><au>Foisner, Roland</au><au>Lattanzi, Giovanna</au><au>Capanni, Cristina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes</atitle><jtitle>Oncotarget</jtitle><addtitle>Oncotarget</addtitle><date>2016-03-29</date><risdate>2016</risdate><volume>7</volume><issue>13</issue><spage>15662</spage><epage>15677</epage><pages>15662-15677</pages><issn>1949-2553</issn><eissn>1949-2553</eissn><abstract>Chromatin disorganization is one of the major alterations linked to prelamin A processing impairment. In this study we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure. We show that when prelamin A and BAF cannot properly interact no prelamin A-dependent effects on chromatin occur; similar to what is observed in human Nestor Guillermo Progeria Syndrome cells harboring a BAF mutation, in HEK293 cells expressing a BAF mutant unable to bind prelamin A, or in siRNA mediated BAF-depleted HEK293 cells expressing prelamin A. BAF is necessary to induce histone trimethyl-H3K9 as well as HP1-alpha and LAP2-alpha nuclear relocalization in response to prelamin A accumulation. These findings are enforced by electron microscopy evaluations showing how the prelamin A-BAF interaction governs overall chromatin organization. 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| subjects | Chromatin - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism HEK293 Cells Humans Lamin Type A - metabolism Mutation Nuclear Proteins - genetics Nuclear Proteins - metabolism Progeria - genetics Progeria - metabolism Progeria - pathology Research Paper |
| title | Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes |
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