Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6
As an indispensable structure protein, the herpes simplex virus 1 (HSV-1) UL6 has been described to exert numerous roles in viral proliferation. However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent...
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Veröffentlicht in: | Aging (Albany, NY.) NY.), 2020-04, Vol.12 (7), p.5751-5763 |
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creator | Cai, Mingsheng Ou, Xiaowen Li, Yiwen Zou, Xingmei Xu, Zuo Wang, Yuanfang Peng, Hao Deng, Yangxi Guo, Yingjie Lu, Manjiao Gan, Weidong Peng, Tao Li, Meili |
description | As an indispensable structure protein, the herpes simplex virus 1 (HSV-1) UL6 has been described to exert numerous roles in viral proliferation. However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent microscopy, UL6 was shown to mainly locate in the nucleus in enhanced yellow fluorescent protein or Flag tag fused expression plasmid-transfected cells or HSV-1-infected cells, whereas its predicted nuclear localization signal was nonfunctional. In addition, by exploiting dominant negative mutant and inhibitor of different nuclear import receptors, as well as co-immunoprecipitation and RNA interference assays, UL6 was established to interact with importin alpha 1, importin alpha 7 and transportin-1 to mediate its nuclear translocation under the help of Ran-mediated GTP hydrolysis. Accordingly, these results will advance the knowledge of UL6-mediated biological significances in HSV-1 infection cycle. |
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However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent microscopy, UL6 was shown to mainly locate in the nucleus in enhanced yellow fluorescent protein or Flag tag fused expression plasmid-transfected cells or HSV-1-infected cells, whereas its predicted nuclear localization signal was nonfunctional. In addition, by exploiting dominant negative mutant and inhibitor of different nuclear import receptors, as well as co-immunoprecipitation and RNA interference assays, UL6 was established to interact with importin alpha 1, importin alpha 7 and transportin-1 to mediate its nuclear translocation under the help of Ran-mediated GTP hydrolysis. Accordingly, these results will advance the knowledge of UL6-mediated biological significances in HSV-1 infection cycle.</description><identifier>ISSN: 1945-4589</identifier><identifier>EISSN: 1945-4589</identifier><identifier>DOI: 10.18632/aging.102965</identifier><identifier>PMID: 32235005</identifier><language>eng</language><publisher>ORCHARD PARK: Impact Journals Llc</publisher><subject>Active Transport, Cell Nucleus - physiology ; Animals ; Cell Biology ; Cell Nucleus - metabolism ; Chlorocebus aethiops ; COS Cells ; Geriatrics & Gerontology ; HEK293 Cells ; Herpesvirus 1, Human - metabolism ; Humans ; Life Sciences & Biomedicine ; Research Paper ; Science & Technology ; Viral Proteins - metabolism</subject><ispartof>Aging (Albany, NY.), 2020-04, Vol.12 (7), p.5751-5763</ispartof><rights>Copyright © 2020 Cai et al.</rights><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>8</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000526933400011</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c453t-cef0181e605fe7870a210c27ecd35ede6f6b300d025b732e166dda753992cf3f3</citedby><cites>FETCH-LOGICAL-c453t-cef0181e605fe7870a210c27ecd35ede6f6b300d025b732e166dda753992cf3f3</cites><orcidid>0000-0001-5260-7128</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/PMC7185102/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185102/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,28253,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32235005$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cai, Mingsheng</creatorcontrib><creatorcontrib>Ou, Xiaowen</creatorcontrib><creatorcontrib>Li, Yiwen</creatorcontrib><creatorcontrib>Zou, Xingmei</creatorcontrib><creatorcontrib>Xu, Zuo</creatorcontrib><creatorcontrib>Wang, Yuanfang</creatorcontrib><creatorcontrib>Peng, Hao</creatorcontrib><creatorcontrib>Deng, Yangxi</creatorcontrib><creatorcontrib>Guo, Yingjie</creatorcontrib><creatorcontrib>Lu, Manjiao</creatorcontrib><creatorcontrib>Gan, Weidong</creatorcontrib><creatorcontrib>Peng, Tao</creatorcontrib><creatorcontrib>Li, Meili</creatorcontrib><title>Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6</title><title>Aging (Albany, NY.)</title><addtitle>AGING-US</addtitle><addtitle>Aging (Albany NY)</addtitle><description>As an indispensable structure protein, the herpes simplex virus 1 (HSV-1) UL6 has been described to exert numerous roles in viral proliferation. However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent microscopy, UL6 was shown to mainly locate in the nucleus in enhanced yellow fluorescent protein or Flag tag fused expression plasmid-transfected cells or HSV-1-infected cells, whereas its predicted nuclear localization signal was nonfunctional. In addition, by exploiting dominant negative mutant and inhibitor of different nuclear import receptors, as well as co-immunoprecipitation and RNA interference assays, UL6 was established to interact with importin alpha 1, importin alpha 7 and transportin-1 to mediate its nuclear translocation under the help of Ran-mediated GTP hydrolysis. Accordingly, these results will advance the knowledge of UL6-mediated biological significances in HSV-1 infection cycle.</description><subject>Active Transport, Cell Nucleus - physiology</subject><subject>Animals</subject><subject>Cell Biology</subject><subject>Cell Nucleus - metabolism</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Geriatrics & Gerontology</subject><subject>HEK293 Cells</subject><subject>Herpesvirus 1, Human - metabolism</subject><subject>Humans</subject><subject>Life Sciences & Biomedicine</subject><subject>Research Paper</subject><subject>Science & Technology</subject><subject>Viral Proteins - metabolism</subject><issn>1945-4589</issn><issn>1945-4589</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><recordid>eNqNkUtv1DAUhS1ERUthyRZ5iYTS-hE7yQYJjXhJU3VD15bjXM8YOfZgOy3l1-POlFHZsfKVzneOr-5B6A0lF7SXnF3qjQubC0rYIMUzdEaHVjSt6IfnT-ZT9DLnH4RIIVr5Ap1yxrggRJwhfxU9mMXrhHXQJc73OFpctoDzMhrwfi_5aLR3v3VxMVRuwmExHqrg5l1MBc9gtjq4PD-Yt5B2kHGumodf-NalJWOKb9byFTqx2md4_fieo5vPn76vvjbr6y_fVh_XjWkFL40BS2hPQRJhoes7ohklhnVgJi5gAmnlyAmZCBNjxxlQKadJd4IPAzOWW36OPhxyd8s4w2QglKS92iU363SvonbqXyW4rdrEW9XRXtRL1oB3jwEp_lwgFzW7_HANHSAuWTHei45T3g4VbQ6oSTHnBPb4DSVq35DaN6QODVX-7dPdjvTfSirQH4A7GKPNxkEwcMRIRZgcOG_rROnKlX0pq7iEUq3v_9_K_wCpIrBa</recordid><startdate>20200401</startdate><enddate>20200401</enddate><creator>Cai, Mingsheng</creator><creator>Ou, Xiaowen</creator><creator>Li, Yiwen</creator><creator>Zou, Xingmei</creator><creator>Xu, Zuo</creator><creator>Wang, Yuanfang</creator><creator>Peng, Hao</creator><creator>Deng, Yangxi</creator><creator>Guo, Yingjie</creator><creator>Lu, Manjiao</creator><creator>Gan, Weidong</creator><creator>Peng, Tao</creator><creator>Li, Meili</creator><general>Impact Journals Llc</general><general>Impact Journals</general><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5260-7128</orcidid></search><sort><creationdate>20200401</creationdate><title>Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6</title><author>Cai, Mingsheng ; Ou, Xiaowen ; Li, Yiwen ; Zou, Xingmei ; Xu, Zuo ; Wang, Yuanfang ; Peng, Hao ; Deng, Yangxi ; Guo, Yingjie ; Lu, Manjiao ; Gan, Weidong ; Peng, Tao ; Li, Meili</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-cef0181e605fe7870a210c27ecd35ede6f6b300d025b732e166dda753992cf3f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Active Transport, Cell Nucleus - physiology</topic><topic>Animals</topic><topic>Cell Biology</topic><topic>Cell Nucleus - metabolism</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Geriatrics & Gerontology</topic><topic>HEK293 Cells</topic><topic>Herpesvirus 1, Human - metabolism</topic><topic>Humans</topic><topic>Life Sciences & Biomedicine</topic><topic>Research Paper</topic><topic>Science & Technology</topic><topic>Viral Proteins - metabolism</topic><toplevel>online_resources</toplevel><creatorcontrib>Cai, Mingsheng</creatorcontrib><creatorcontrib>Ou, Xiaowen</creatorcontrib><creatorcontrib>Li, Yiwen</creatorcontrib><creatorcontrib>Zou, Xingmei</creatorcontrib><creatorcontrib>Xu, Zuo</creatorcontrib><creatorcontrib>Wang, Yuanfang</creatorcontrib><creatorcontrib>Peng, Hao</creatorcontrib><creatorcontrib>Deng, Yangxi</creatorcontrib><creatorcontrib>Guo, Yingjie</creatorcontrib><creatorcontrib>Lu, Manjiao</creatorcontrib><creatorcontrib>Gan, Weidong</creatorcontrib><creatorcontrib>Peng, Tao</creatorcontrib><creatorcontrib>Li, Meili</creatorcontrib><collection>Web of Science - Science Citation Index Expanded - 2020</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><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>Aging (Albany, NY.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cai, Mingsheng</au><au>Ou, Xiaowen</au><au>Li, Yiwen</au><au>Zou, Xingmei</au><au>Xu, Zuo</au><au>Wang, Yuanfang</au><au>Peng, Hao</au><au>Deng, Yangxi</au><au>Guo, Yingjie</au><au>Lu, Manjiao</au><au>Gan, Weidong</au><au>Peng, Tao</au><au>Li, Meili</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6</atitle><jtitle>Aging (Albany, NY.)</jtitle><stitle>AGING-US</stitle><addtitle>Aging (Albany NY)</addtitle><date>2020-04-01</date><risdate>2020</risdate><volume>12</volume><issue>7</issue><spage>5751</spage><epage>5763</epage><pages>5751-5763</pages><issn>1945-4589</issn><eissn>1945-4589</eissn><abstract>As an indispensable structure protein, the herpes simplex virus 1 (HSV-1) UL6 has been described to exert numerous roles in viral proliferation. However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent microscopy, UL6 was shown to mainly locate in the nucleus in enhanced yellow fluorescent protein or Flag tag fused expression plasmid-transfected cells or HSV-1-infected cells, whereas its predicted nuclear localization signal was nonfunctional. In addition, by exploiting dominant negative mutant and inhibitor of different nuclear import receptors, as well as co-immunoprecipitation and RNA interference assays, UL6 was established to interact with importin alpha 1, importin alpha 7 and transportin-1 to mediate its nuclear translocation under the help of Ran-mediated GTP hydrolysis. 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subjects | Active Transport, Cell Nucleus - physiology Animals Cell Biology Cell Nucleus - metabolism Chlorocebus aethiops COS Cells Geriatrics & Gerontology HEK293 Cells Herpesvirus 1, Human - metabolism Humans Life Sciences & Biomedicine Research Paper Science & Technology Viral Proteins - metabolism |
title | Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6 |
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