Activation of non-canonical NF-κB pathway mediated by STP-A11, an oncoprotein of Herpesvirus saimiri
Abstract Although Saimiri Transforming Protein (STP)-A11, an oncoprotein of Herpesvirus saimiri , has been known to activate NF-κB signaling pathway, the detailed mechanism has not been reported yet. We herein report that STP-A11 activates non-canonical NF-κB pathway, resulting in p100 processing to...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2007-03, Vol.359 (1), p.37-45 |
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| container_title | Virology (New York, N.Y.) |
| container_volume | 359 |
| creator | Cho, Il-Rae Jeong, Sunam Jhun, Byung Hak An, Won G Lee, BokSoo Kwak, Youn-Tae Lee, Sun-Hwa Jung, Jae U Chung, Young-Hwa |
| description | Abstract Although Saimiri Transforming Protein (STP)-A11, an oncoprotein of Herpesvirus saimiri , has been known to activate NF-κB signaling pathway, the detailed mechanism has not been reported yet. We herein report that STP-A11 activates non-canonical NF-κB pathway, resulting in p100 processing to p52. In addition, translocation of p52 protein (NF-κB2) into the nucleus is observed by the expression of STP-A11. STP-A11-mediated processing of p100 to p52 protein requires proteosome-mediated proteolysis because MG132 treatment clearly blocked p52 production in spite of the expression of STP-A11. Analysis of STP-A11 mutants to activate NF-κB2 pathway discloses the requirement of TRAF6-binding site not Src-binding site for STP-A11-mediated NF-κB2 pathway. Blockage of STP-A11-mediated p52 production using siRNA against p52 enhanced a chemotherapeutic drug-mediated cell death, suggesting that p52 production induced by the expression of STP-A11 would contribute to cellular transformation, which results from a resistance to cell death. |
| doi_str_mv | 10.1016/j.virol.2006.09.001 |
| format | Article |
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We herein report that STP-A11 activates non-canonical NF-κB pathway, resulting in p100 processing to p52. In addition, translocation of p52 protein (NF-κB2) into the nucleus is observed by the expression of STP-A11. STP-A11-mediated processing of p100 to p52 protein requires proteosome-mediated proteolysis because MG132 treatment clearly blocked p52 production in spite of the expression of STP-A11. Analysis of STP-A11 mutants to activate NF-κB2 pathway discloses the requirement of TRAF6-binding site not Src-binding site for STP-A11-mediated NF-κB2 pathway. Blockage of STP-A11-mediated p52 production using siRNA against p52 enhanced a chemotherapeutic drug-mediated cell death, suggesting that p52 production induced by the expression of STP-A11 would contribute to cellular transformation, which results from a resistance to cell death.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2006.09.001</identifier><language>eng</language><publisher>Elsevier Inc</publisher><subject>Canonical NF-κB ; Herpesvirus saimiri ; IKK ; Infectious Disease ; NF-κB2 ; NIK ; Non-canonical NF-κB ; p100 processing ; p52 protein ; STP-A11</subject><ispartof>Virology (New York, N.Y.), 2007-03, Vol.359 (1), p.37-45</ispartof><rights>Elsevier Inc.</rights><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-ccb639a29cb4479e2dbf4f499c8d02d95db6beb04bfd30868ac03cdd842bb1e83</citedby><cites>FETCH-LOGICAL-c389t-ccb639a29cb4479e2dbf4f499c8d02d95db6beb04bfd30868ac03cdd842bb1e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2006.09.001$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids></links><search><creatorcontrib>Cho, Il-Rae</creatorcontrib><creatorcontrib>Jeong, Sunam</creatorcontrib><creatorcontrib>Jhun, Byung Hak</creatorcontrib><creatorcontrib>An, Won G</creatorcontrib><creatorcontrib>Lee, BokSoo</creatorcontrib><creatorcontrib>Kwak, Youn-Tae</creatorcontrib><creatorcontrib>Lee, Sun-Hwa</creatorcontrib><creatorcontrib>Jung, Jae U</creatorcontrib><creatorcontrib>Chung, Young-Hwa</creatorcontrib><title>Activation of non-canonical NF-κB pathway mediated by STP-A11, an oncoprotein of Herpesvirus saimiri</title><title>Virology (New York, N.Y.)</title><description>Abstract Although Saimiri Transforming Protein (STP)-A11, an oncoprotein of Herpesvirus saimiri , has been known to activate NF-κB signaling pathway, the detailed mechanism has not been reported yet. 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Blockage of STP-A11-mediated p52 production using siRNA against p52 enhanced a chemotherapeutic drug-mediated cell death, suggesting that p52 production induced by the expression of STP-A11 would contribute to cellular transformation, which results from a resistance to cell death.</description><subject>Canonical NF-κB</subject><subject>Herpesvirus saimiri</subject><subject>IKK</subject><subject>Infectious Disease</subject><subject>NF-κB2</subject><subject>NIK</subject><subject>Non-canonical NF-κB</subject><subject>p100 processing</subject><subject>p52 protein</subject><subject>STP-A11</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkc1uEzEQx62KSoSWJ-DiEyd2GX_UWR9AChWlSFVBaiv1ZvljVnXYrIO9Ccqr8RA8E07CiUsvY400v7_GvyHkDYOWAVPvl-025jS0HEC1oFsAdkJmDLRqQEj2gswAJG9Ux_lL8qqUJdR-PocZwYWf4tZOMY009XRMY-NtrdHbgd5eNX9-f6JrOz39sju6whDthIG6Hb27_94sGHtHbeVGn9Y5TRgPGdeY11jqQptCi42rmOM5Oe3tUPD1v_eMPFx9vr-8bm6-ffl6ubhpvOj01HjvlNCWa--knGvkwfWyl1r7LgAP-iI45dCBdH0Q0KnOehA-hE5y5xh24oy8PebWdX5usExmFYvHYbAjpk0xTF_Ma7Cqg-I46HMqJWNv1jmubN4ZBmav1CzNQanZKzWgTVVaqQ9HCusfthGzKT7i6KuXjH4yIcVn-I__8X6IB9U_cIdlmTZ5rHoMM4UbMHf7o-1vBqqGSPEo_gI4FZdM</recordid><startdate>20070301</startdate><enddate>20070301</enddate><creator>Cho, Il-Rae</creator><creator>Jeong, Sunam</creator><creator>Jhun, Byung Hak</creator><creator>An, Won G</creator><creator>Lee, BokSoo</creator><creator>Kwak, Youn-Tae</creator><creator>Lee, Sun-Hwa</creator><creator>Jung, Jae U</creator><creator>Chung, Young-Hwa</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TO</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20070301</creationdate><title>Activation of non-canonical NF-κB pathway mediated by STP-A11, an oncoprotein of Herpesvirus saimiri</title><author>Cho, Il-Rae ; Jeong, Sunam ; Jhun, Byung Hak ; An, Won G ; Lee, BokSoo ; Kwak, Youn-Tae ; Lee, Sun-Hwa ; Jung, Jae U ; Chung, Young-Hwa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-ccb639a29cb4479e2dbf4f499c8d02d95db6beb04bfd30868ac03cdd842bb1e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Canonical NF-κB</topic><topic>Herpesvirus saimiri</topic><topic>IKK</topic><topic>Infectious Disease</topic><topic>NF-κB2</topic><topic>NIK</topic><topic>Non-canonical NF-κB</topic><topic>p100 processing</topic><topic>p52 protein</topic><topic>STP-A11</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cho, Il-Rae</creatorcontrib><creatorcontrib>Jeong, Sunam</creatorcontrib><creatorcontrib>Jhun, Byung Hak</creatorcontrib><creatorcontrib>An, Won G</creatorcontrib><creatorcontrib>Lee, BokSoo</creatorcontrib><creatorcontrib>Kwak, Youn-Tae</creatorcontrib><creatorcontrib>Lee, Sun-Hwa</creatorcontrib><creatorcontrib>Jung, Jae U</creatorcontrib><creatorcontrib>Chung, Young-Hwa</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>CrossRef</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cho, Il-Rae</au><au>Jeong, Sunam</au><au>Jhun, Byung Hak</au><au>An, Won G</au><au>Lee, BokSoo</au><au>Kwak, Youn-Tae</au><au>Lee, Sun-Hwa</au><au>Jung, Jae U</au><au>Chung, Young-Hwa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of non-canonical NF-κB pathway mediated by STP-A11, an oncoprotein of Herpesvirus saimiri</atitle><jtitle>Virology (New York, N.Y.)</jtitle><date>2007-03-01</date><risdate>2007</risdate><volume>359</volume><issue>1</issue><spage>37</spage><epage>45</epage><pages>37-45</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract Although Saimiri Transforming Protein (STP)-A11, an oncoprotein of Herpesvirus saimiri , has been known to activate NF-κB signaling pathway, the detailed mechanism has not been reported yet. We herein report that STP-A11 activates non-canonical NF-κB pathway, resulting in p100 processing to p52. In addition, translocation of p52 protein (NF-κB2) into the nucleus is observed by the expression of STP-A11. STP-A11-mediated processing of p100 to p52 protein requires proteosome-mediated proteolysis because MG132 treatment clearly blocked p52 production in spite of the expression of STP-A11. Analysis of STP-A11 mutants to activate NF-κB2 pathway discloses the requirement of TRAF6-binding site not Src-binding site for STP-A11-mediated NF-κB2 pathway. Blockage of STP-A11-mediated p52 production using siRNA against p52 enhanced a chemotherapeutic drug-mediated cell death, suggesting that p52 production induced by the expression of STP-A11 would contribute to cellular transformation, which results from a resistance to cell death.</abstract><pub>Elsevier Inc</pub><doi>10.1016/j.virol.2006.09.001</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Canonical NF-κB Herpesvirus saimiri IKK Infectious Disease NF-κB2 NIK Non-canonical NF-κB p100 processing p52 protein STP-A11 |
| title | Activation of non-canonical NF-κB pathway mediated by STP-A11, an oncoprotein of Herpesvirus saimiri |
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