TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion
Abstract TULA, a recently identified UBA- and SH3-containing protein, has previously been shown to regulate cell signaling through protein tyrosine kinases. In order to search for novel functions of TULA, we identified, using mass spectrometry, proteins associated with TULA. ABCE-1 also known as RLI...
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creator | Smirnova, Evgeniya V Collingwood, Therese S Bisbal, Catherine Tsygankova, Oxana M Bogush, Marina Meinkoth, Judy L Henderson, Earl E Annan, Roland S Tsygankov, Alexander Y |
description | Abstract TULA, a recently identified UBA- and SH3-containing protein, has previously been shown to regulate cell signaling through protein tyrosine kinases. In order to search for novel functions of TULA, we identified, using mass spectrometry, proteins associated with TULA. ABCE-1 also known as RLI and HP68, a host factor of HIV-1 assembly, was found among TULA-associated proteins in these experiments. Considering an important role of ABCE-1 in HIV-1 assembly, we were compelled to analyze the effect of TULA on HIV-1 biogenesis. Our study provides evidence that TULA proteins substantially inhibit production of both sub-genomic and full-length HIV-1 viral particles and that the effect of TULA is dependent on UBA domain-mediated interactions. The primary role of ABCE-1 in the effect of TULA appears to be the recruitment of TULA to the sites of HIV-1 assembly where TULA interferes with the late steps of the HIV-1 life cycle, most likely by disrupting essential ubiquitylation-dependent events that remain to be identified. |
doi_str_mv | 10.1016/j.virol.2007.10.012 |
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In order to search for novel functions of TULA, we identified, using mass spectrometry, proteins associated with TULA. ABCE-1 also known as RLI and HP68, a host factor of HIV-1 assembly, was found among TULA-associated proteins in these experiments. Considering an important role of ABCE-1 in HIV-1 assembly, we were compelled to analyze the effect of TULA on HIV-1 biogenesis. Our study provides evidence that TULA proteins substantially inhibit production of both sub-genomic and full-length HIV-1 viral particles and that the effect of TULA is dependent on UBA domain-mediated interactions. The primary role of ABCE-1 in the effect of TULA appears to be the recruitment of TULA to the sites of HIV-1 assembly where TULA interferes with the late steps of the HIV-1 life cycle, most likely by disrupting essential ubiquitylation-dependent events that remain to be identified.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2007.10.012</identifier><identifier>PMID: 18006034</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>ABCE-1 ; Amino Acid Sequence ; ATP-Binding Cassette Transporters - chemistry ; ATP-Binding Cassette Transporters - genetics ; ATP-Binding Cassette Transporters - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Line ; Chaperonins - chemistry ; Chaperonins - genetics ; Chaperonins - metabolism ; Gag ; Gene Products, gag - genetics ; Gene Products, gag - metabolism ; HeLa Cells ; HIV-1 ; HIV-1 - drug effects ; HIV-1 - physiology ; Human immunodeficiency virus 1 ; Humans ; Immunoprecipitation ; Infectious Disease ; Mass Spectrometry ; Molecular Sequence Data ; Transfection ; TULA ; UBA ; Ubiquitin ; Ubiquitin - genetics ; Ubiquitin - metabolism ; Virus Assembly</subject><ispartof>Virology (New York, N.Y.), 2008-03, Vol.372 (1), p.10-23</ispartof><rights>Elsevier Inc.</rights><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-d73f5f36730f8083a3b78644db29a09aea205b275582a0a6380008fb5147b8ff3</citedby><cites>FETCH-LOGICAL-c488t-d73f5f36730f8083a3b78644db29a09aea205b275582a0a6380008fb5147b8ff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S004268220700668X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18006034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smirnova, Evgeniya V</creatorcontrib><creatorcontrib>Collingwood, Therese S</creatorcontrib><creatorcontrib>Bisbal, Catherine</creatorcontrib><creatorcontrib>Tsygankova, Oxana M</creatorcontrib><creatorcontrib>Bogush, Marina</creatorcontrib><creatorcontrib>Meinkoth, Judy L</creatorcontrib><creatorcontrib>Henderson, Earl E</creatorcontrib><creatorcontrib>Annan, Roland S</creatorcontrib><creatorcontrib>Tsygankov, Alexander Y</creatorcontrib><title>TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract TULA, a recently identified UBA- and SH3-containing protein, has previously been shown to regulate cell signaling through protein tyrosine kinases. 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The primary role of ABCE-1 in the effect of TULA appears to be the recruitment of TULA to the sites of HIV-1 assembly where TULA interferes with the late steps of the HIV-1 life cycle, most likely by disrupting essential ubiquitylation-dependent events that remain to be identified.</description><subject>ABCE-1</subject><subject>Amino Acid Sequence</subject><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>ATP-Binding Cassette Transporters - genetics</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Chaperonins - chemistry</subject><subject>Chaperonins - genetics</subject><subject>Chaperonins - metabolism</subject><subject>Gag</subject><subject>Gene Products, gag - genetics</subject><subject>Gene Products, gag - metabolism</subject><subject>HeLa Cells</subject><subject>HIV-1</subject><subject>HIV-1 - drug effects</subject><subject>HIV-1 - physiology</subject><subject>Human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Infectious Disease</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Transfection</subject><subject>TULA</subject><subject>UBA</subject><subject>Ubiquitin</subject><subject>Ubiquitin - genetics</subject><subject>Ubiquitin - metabolism</subject><subject>Virus Assembly</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksGO0zAQhi0EYsvCEyAhnziRMraT2DmA1K0WdqVKHNgibpadjKlLapc4rdS3x9lWQuKyJ8sz3_z2zD-EvGUwZ8Dqj9v50Q-xn3MAmSNzYPwZmTFo6gJEyZ6TGUDJi1pxfkVepbSFfJcSXpIrpgDqDM3I8WG9WtD9EEf0IVHrQ0fHSBc3y9uCfaCGbmIaqTPtGAcaHb27_1EwalLCne1PGci8Dxtv_XjJWR9_YcDkU05kgfXNouhwj6HDMCmljY_hNXnhTJ_wzeW8Jusvtw_Lu2L17ev9crEq2lKpseikcJUTtRTgFChhhJWqLsvO8sZAY9BwqCyXVaW4AVOL3BcoZytWSqucE9fk_Vk3d_jngGnUO59a7HsTMB6SlsAb2fDqSZBDzUXDeAbFGWyHmNKATu8HvzPDSTPQky96qx990ZMvUxAeq95d5A92h92_mosRGfh0BjBP4-hx0Kn1GFrs_IDtqLvon3jg83_1be-Db03_G0-YtvEwhDxozXTiGvT3aTWmzQCZP1Crn-IvVQywxQ</recordid><startdate>20080301</startdate><enddate>20080301</enddate><creator>Smirnova, Evgeniya V</creator><creator>Collingwood, Therese S</creator><creator>Bisbal, Catherine</creator><creator>Tsygankova, Oxana M</creator><creator>Bogush, Marina</creator><creator>Meinkoth, Judy L</creator><creator>Henderson, Earl E</creator><creator>Annan, Roland S</creator><creator>Tsygankov, Alexander Y</creator><general>Elsevier Inc</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></search><sort><creationdate>20080301</creationdate><title>TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion</title><author>Smirnova, Evgeniya V ; Collingwood, Therese S ; Bisbal, Catherine ; Tsygankova, Oxana M ; Bogush, Marina ; Meinkoth, Judy L ; Henderson, Earl E ; Annan, Roland S ; Tsygankov, Alexander Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-d73f5f36730f8083a3b78644db29a09aea205b275582a0a6380008fb5147b8ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>ABCE-1</topic><topic>Amino Acid Sequence</topic><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>ATP-Binding Cassette Transporters - genetics</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Chaperonins - chemistry</topic><topic>Chaperonins - genetics</topic><topic>Chaperonins - metabolism</topic><topic>Gag</topic><topic>Gene Products, gag - genetics</topic><topic>Gene Products, gag - metabolism</topic><topic>HeLa Cells</topic><topic>HIV-1</topic><topic>HIV-1 - drug effects</topic><topic>HIV-1 - physiology</topic><topic>Human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Infectious Disease</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Transfection</topic><topic>TULA</topic><topic>UBA</topic><topic>Ubiquitin</topic><topic>Ubiquitin - genetics</topic><topic>Ubiquitin - metabolism</topic><topic>Virus Assembly</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smirnova, Evgeniya V</creatorcontrib><creatorcontrib>Collingwood, Therese S</creatorcontrib><creatorcontrib>Bisbal, Catherine</creatorcontrib><creatorcontrib>Tsygankova, Oxana M</creatorcontrib><creatorcontrib>Bogush, Marina</creatorcontrib><creatorcontrib>Meinkoth, Judy L</creatorcontrib><creatorcontrib>Henderson, Earl E</creatorcontrib><creatorcontrib>Annan, Roland S</creatorcontrib><creatorcontrib>Tsygankov, Alexander Y</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><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smirnova, Evgeniya V</au><au>Collingwood, Therese S</au><au>Bisbal, Catherine</au><au>Tsygankova, Oxana M</au><au>Bogush, Marina</au><au>Meinkoth, Judy L</au><au>Henderson, Earl E</au><au>Annan, Roland S</au><au>Tsygankov, Alexander Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2008-03-01</date><risdate>2008</risdate><volume>372</volume><issue>1</issue><spage>10</spage><epage>23</epage><pages>10-23</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract TULA, a recently identified UBA- and SH3-containing protein, has previously been shown to regulate cell signaling through protein tyrosine kinases. 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The primary role of ABCE-1 in the effect of TULA appears to be the recruitment of TULA to the sites of HIV-1 assembly where TULA interferes with the late steps of the HIV-1 life cycle, most likely by disrupting essential ubiquitylation-dependent events that remain to be identified.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18006034</pmid><doi>10.1016/j.virol.2007.10.012</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | ABCE-1 Amino Acid Sequence ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell Line Chaperonins - chemistry Chaperonins - genetics Chaperonins - metabolism Gag Gene Products, gag - genetics Gene Products, gag - metabolism HeLa Cells HIV-1 HIV-1 - drug effects HIV-1 - physiology Human immunodeficiency virus 1 Humans Immunoprecipitation Infectious Disease Mass Spectrometry Molecular Sequence Data Transfection TULA UBA Ubiquitin Ubiquitin - genetics Ubiquitin - metabolism Virus Assembly |
title | TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion |
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