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Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration
Retroviral infection triggers the cytoplasmic translocation of two Crm1-dependent shuttle factors, namely the Ini1 (integrase interactor 1, hSNF5) and the promyelocytic leukemia (PML) protein. Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integrati...
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Published in: | FEBS letters 2004-12, Vol.578 (3), p.291-296 |
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description | Retroviral infection triggers the cytoplasmic translocation of two Crm1-dependent shuttle factors, namely the Ini1 (integrase interactor 1, hSNF5) and the promyelocytic leukemia (PML) protein. Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. Furthermore, Ini1 does not interfere with retroviral integration, as cells lacking Ini1 show no increased infection susceptibility. |
doi_str_mv | 10.1016/j.febslet.2004.11.016 |
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Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. 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Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. Furthermore, Ini1 does not interfere with retroviral integration, as cells lacking Ini1 show no increased infection susceptibility.</description><subject>Annexin A5</subject><subject>Annexin A5 - metabolism</subject><subject>Antibiotics, Antineoplastic</subject><subject>Antibiotics, Antineoplastic - pharmacology</subject><subject>Blotting, Western</subject><subject>Cell Fractionation</subject><subject>Chromosomal Proteins, Non-Histone</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>DNA-Binding Proteins</subject><subject>DNA-Binding Proteins - drug effects</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>double-stranded RNA</subject><subject>dsRNA</subject><subject>EGFP</subject><subject>enhanced green fluorescence protein</subject><subject>FACS</subject><subject>Fatty Acids, Unsaturated</subject><subject>Fatty Acids, Unsaturated - pharmacology</subject><subject>fluorescence activated cell sorting</subject><subject>Fluorescent Antibody Technique</subject><subject>HeLa Cells</subject><subject>HIV</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Ini1</subject><subject>integrase interactor 1</subject><subject>Integrase interactor 1/hSNF5</subject><subject>leptomycin B</subject><subject>Life Sciences</subject><subject>LMB</subject><subject>Microbiology and Parasitology</subject><subject>Neoplasm Proteins</subject><subject>Neoplasm Proteins - biosynthesis</subject><subject>Neoplasm Proteins - drug effects</subject><subject>Nuclear Proteins</subject><subject>Nuclear Proteins - biosynthesis</subject><subject>Nuclear Proteins - drug effects</subject><subject>PBS</subject><subject>phosphate-buffered saline</subject><subject>PIC</subject><subject>PML</subject><subject>PML oncogenic domain</subject><subject>POD</subject><subject>Polymerase Chain Reaction</subject><subject>preintegration complex</subject><subject>Promyelocytic Leukemia Protein</subject><subject>propidium iodide</subject><subject>Retroviral integration</subject><subject>Retroviridae Infections</subject><subject>Retroviridae Infections - enzymology</subject><subject>Retroviridae Infections - metabolism</subject><subject>RNA Interference</subject><subject>RNAi</subject><subject>siRNA</subject><subject>small inhibitory RNA</subject><subject>SMARCB1 Protein</subject><subject>Transcription Factors</subject><subject>Transcription Factors - biosynthesis</subject><subject>Transcription Factors - drug effects</subject><subject>Tumor Suppressor Proteins</subject><subject>vesicular stomatitis virus glycoprotein</subject><subject>Virology</subject><subject>Virus Integration</subject><subject>Virus Integration - physiology</subject><subject>VSV-G</subject><subject>wild type</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqNkk1vEzEQhlcIREPhJ4B84rZbj-21vSdUqoZUCh9S4WxtvGPiaLMO9m5K_j1OE8GxnKwZPfN6rMdF8RZoBRTk1aZyuEo9jhWjVFQAVe4-K2agFS-5kPp5MaMURFmrhl8Ur1La0FxraF4WF1DXutG8nhW_7wYPV-v7L_Oa-EQ6n3Y4pHbVI3EhkohjDHsfp1T6oZssdsQexrDr27T1lrTWTtupb0cfBhIc-fZ5SdqhI13ARIYwEj-MGB1GJA9-XD-WP-Mj_rp44do-4ZvzeVn8mN9-v1mUy6-f7m6ul6UVjdKlYyBFJxiTjWsAwXKKSmq1EpoLkIw5qzRXVLD8NoXScckslyuUtdNWKn5ZlKfcddubXfTbNh5MaL1ZXC_Nrk0jTtFQqmvKJOwh8-9P_C6GXxOm0Wx9stj37YBhSkYqULJmzZMgNIo2WosM1ifQxpBSRPd3DaDm6NJszNmlObo0ACZ389y78wXTaovdv6mzvAwsTsCD7_Hwf6lmfvuR3R8_xvFfUEGBa6pz1IdTFGYVe4_RJOtxyL59RDuaLvgntv0DRD7HYw</recordid><startdate>20041217</startdate><enddate>20041217</enddate><creator>Boese, Annette</creator><creator>Sommer, Peter</creator><creator>Gaussin, Armelle</creator><creator>Reimann, Andreas</creator><creator>Nehrbass, Ulf</creator><general>Elsevier B.V</general><general>Wiley</general><scope>6I.</scope><scope>AAFTH</scope><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>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope></search><sort><creationdate>20041217</creationdate><title>Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration</title><author>Boese, Annette ; Sommer, Peter ; Gaussin, Armelle ; Reimann, Andreas ; Nehrbass, Ulf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4978-f2164d42269f91e1c30e7687b48341622fc78370420187e6f362c36be65f8c673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Annexin A5</topic><topic>Annexin A5 - metabolism</topic><topic>Antibiotics, Antineoplastic</topic><topic>Antibiotics, Antineoplastic - pharmacology</topic><topic>Blotting, Western</topic><topic>Cell Fractionation</topic><topic>Chromosomal Proteins, Non-Histone</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>DNA-Binding Proteins</topic><topic>DNA-Binding Proteins - drug effects</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>double-stranded RNA</topic><topic>dsRNA</topic><topic>EGFP</topic><topic>enhanced green fluorescence protein</topic><topic>FACS</topic><topic>Fatty Acids, Unsaturated</topic><topic>Fatty Acids, Unsaturated - pharmacology</topic><topic>fluorescence activated cell sorting</topic><topic>Fluorescent Antibody Technique</topic><topic>HeLa Cells</topic><topic>HIV</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Ini1</topic><topic>integrase interactor 1</topic><topic>Integrase interactor 1/hSNF5</topic><topic>leptomycin B</topic><topic>Life Sciences</topic><topic>LMB</topic><topic>Microbiology and Parasitology</topic><topic>Neoplasm Proteins</topic><topic>Neoplasm Proteins - biosynthesis</topic><topic>Neoplasm Proteins - drug effects</topic><topic>Nuclear Proteins</topic><topic>Nuclear Proteins - biosynthesis</topic><topic>Nuclear Proteins - drug effects</topic><topic>PBS</topic><topic>phosphate-buffered saline</topic><topic>PIC</topic><topic>PML</topic><topic>PML oncogenic domain</topic><topic>POD</topic><topic>Polymerase Chain Reaction</topic><topic>preintegration complex</topic><topic>Promyelocytic Leukemia Protein</topic><topic>propidium iodide</topic><topic>Retroviral integration</topic><topic>Retroviridae Infections</topic><topic>Retroviridae Infections - enzymology</topic><topic>Retroviridae Infections - metabolism</topic><topic>RNA Interference</topic><topic>RNAi</topic><topic>siRNA</topic><topic>small inhibitory RNA</topic><topic>SMARCB1 Protein</topic><topic>Transcription Factors</topic><topic>Transcription Factors - biosynthesis</topic><topic>Transcription Factors - drug effects</topic><topic>Tumor Suppressor Proteins</topic><topic>vesicular stomatitis virus glycoprotein</topic><topic>Virology</topic><topic>Virus Integration</topic><topic>Virus Integration - physiology</topic><topic>VSV-G</topic><topic>wild type</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boese, Annette</creatorcontrib><creatorcontrib>Sommer, Peter</creatorcontrib><creatorcontrib>Gaussin, Armelle</creatorcontrib><creatorcontrib>Reimann, Andreas</creatorcontrib><creatorcontrib>Nehrbass, Ulf</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boese, Annette</au><au>Sommer, Peter</au><au>Gaussin, Armelle</au><au>Reimann, Andreas</au><au>Nehrbass, Ulf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-12-17</date><risdate>2004</risdate><volume>578</volume><issue>3</issue><spage>291</spage><epage>296</epage><pages>291-296</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Retroviral infection triggers the cytoplasmic translocation of two Crm1-dependent shuttle factors, namely the Ini1 (integrase interactor 1, hSNF5) and the promyelocytic leukemia (PML) protein. Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. Furthermore, Ini1 does not interfere with retroviral integration, as cells lacking Ini1 show no increased infection susceptibility.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15589835</pmid><doi>10.1016/j.febslet.2004.11.016</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Annexin A5 Annexin A5 - metabolism Antibiotics, Antineoplastic Antibiotics, Antineoplastic - pharmacology Blotting, Western Cell Fractionation Chromosomal Proteins, Non-Histone Cytoplasm Cytoplasm - metabolism DNA-Binding Proteins DNA-Binding Proteins - drug effects DNA-Binding Proteins - metabolism double-stranded RNA dsRNA EGFP enhanced green fluorescence protein FACS Fatty Acids, Unsaturated Fatty Acids, Unsaturated - pharmacology fluorescence activated cell sorting Fluorescent Antibody Technique HeLa Cells HIV Human immunodeficiency virus Humans Ini1 integrase interactor 1 Integrase interactor 1/hSNF5 leptomycin B Life Sciences LMB Microbiology and Parasitology Neoplasm Proteins Neoplasm Proteins - biosynthesis Neoplasm Proteins - drug effects Nuclear Proteins Nuclear Proteins - biosynthesis Nuclear Proteins - drug effects PBS phosphate-buffered saline PIC PML PML oncogenic domain POD Polymerase Chain Reaction preintegration complex Promyelocytic Leukemia Protein propidium iodide Retroviral integration Retroviridae Infections Retroviridae Infections - enzymology Retroviridae Infections - metabolism RNA Interference RNAi siRNA small inhibitory RNA SMARCB1 Protein Transcription Factors Transcription Factors - biosynthesis Transcription Factors - drug effects Tumor Suppressor Proteins vesicular stomatitis virus glycoprotein Virology Virus Integration Virus Integration - physiology VSV-G wild type |
title | Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration |
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