Proteins Related to the Nedd4 Family of Ubiquitin Protein Ligases Interact with the L Domain of Rous Sarcoma Virus and are Required for Gag Budding from Cells
The late assembly (L) domain of retrovirus Gag, required in the final steps of budding for efficient exit from the host cell, is thought to mediate its function through interaction with unknown cellular factors. Here, we report the identification of the Nedd4-1ike family of E3 ubiquitin protein liga...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2001-09, Vol.98 (20), p.11199-11204 |
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| creator | Kikonyogo, Alexandra Bouamr, Fadila Vana, Marcy L. Xiang, Yan Aiyar, Ashok Carter, Carol Leis, Jonathan |
| description | The late assembly (L) domain of retrovirus Gag, required in the final steps of budding for efficient exit from the host cell, is thought to mediate its function through interaction with unknown cellular factors. Here, we report the identification of the Nedd4-1ike family of E3 ubiquitin protein ligases as proteins that specifically interact with the Rous sarcoma virus (RSV) L domain in vitro and in vivo. We screened a chicken embryo cDNA expression library by using a peptide derived from the RSV p2b sequence, isolating two unique partial cDNA clones. Neither clone interacted with a peptide containing mutations known to disrupt in vivo RSV L domain function or with human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) L domain-derived peptides. The WW domain region of one of the clones, late domain-interacting protein 1 (LDI-1), but not the C2 domain, bound RSV Gag and inhibited RSV Gag budding from human 293 cells in a dominant-negative manner, functionally implicating LDI-1 in RSV particle budding from cells. RSV Gag can be coimmune precipitated from cell extracts with an antisera directed at an exogenously expressed hemagglutinin (HA)-tagged LDI-1 or endogenous Nedd4 proteins. These findings mechanistically link the cellular ubiquitination pathway to retrovirus budding. |
| doi_str_mv | 10.1073/pnas.201268998 |
| format | Article |
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Here, we report the identification of the Nedd4-1ike family of E3 ubiquitin protein ligases as proteins that specifically interact with the Rous sarcoma virus (RSV) L domain in vitro and in vivo. We screened a chicken embryo cDNA expression library by using a peptide derived from the RSV p2b sequence, isolating two unique partial cDNA clones. Neither clone interacted with a peptide containing mutations known to disrupt in vivo RSV L domain function or with human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) L domain-derived peptides. The WW domain region of one of the clones, late domain-interacting protein 1 (LDI-1), but not the C2 domain, bound RSV Gag and inhibited RSV Gag budding from human 293 cells in a dominant-negative manner, functionally implicating LDI-1 in RSV particle budding from cells. RSV Gag can be coimmune precipitated from cell extracts with an antisera directed at an exogenously expressed hemagglutinin (HA)-tagged LDI-1 or endogenous Nedd4 proteins. These findings mechanistically link the cellular ubiquitination pathway to retrovirus budding.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.201268998</identifier><identifier>PMID: 11562473</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Antibodies ; Avian Sarcoma Viruses - genetics ; Avian Sarcoma Viruses - metabolism ; Binding Sites ; Biochemistry ; Biological Sciences ; Budding ; Calcium-Binding Proteins - metabolism ; Cell Line ; Cell lines ; Cells ; Chick Embryo ; Cloning, Molecular ; Complementary DNA ; COS cells ; DNA, Complementary ; Endosomal Sorting Complexes Required for Transport ; Equine infectious anemia virus ; gag protein ; Gene Library ; Gene Products, gag - chemistry ; Gene Products, gag - genetics ; Gene Products, gag - metabolism ; Genes, gag ; HIV 1 ; HIV-1 - metabolism ; Human immunodeficiency virus 1 ; Humans ; Infectious Anemia Virus, Equine - metabolism ; late domain-interacting protein 1 ; Ligases - metabolism ; Mathematical functions ; Nedd4 protein ; Nedd4 Ubiquitin Protein Ligases ; Plasmids ; Proteins ; Recombinant Proteins - metabolism ; Rous sarcoma virus ; Transfection ; ubiquitin-protein ligase ; Ubiquitin-Protein Ligases ; Ubiquitins ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2001-09, Vol.98 (20), p.11199-11204</ispartof><rights>Copyright 1993-2001 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Sep 25, 2001</rights><rights>Copyright © 2001, The National Academy of Sciences 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-58f19996137f48f2a3778137efd64724a9241bbba5120ff706fb836d3539f1823</citedby><cites>FETCH-LOGICAL-c520t-58f19996137f48f2a3778137efd64724a9241bbba5120ff706fb836d3539f1823</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/98/20.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3056692$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3056692$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11562473$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kikonyogo, Alexandra</creatorcontrib><creatorcontrib>Bouamr, Fadila</creatorcontrib><creatorcontrib>Vana, Marcy L.</creatorcontrib><creatorcontrib>Xiang, Yan</creatorcontrib><creatorcontrib>Aiyar, Ashok</creatorcontrib><creatorcontrib>Carter, Carol</creatorcontrib><creatorcontrib>Leis, Jonathan</creatorcontrib><title>Proteins Related to the Nedd4 Family of Ubiquitin Protein Ligases Interact with the L Domain of Rous Sarcoma Virus and are Required for Gag Budding from Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The late assembly (L) domain of retrovirus Gag, required in the final steps of budding for efficient exit from the host cell, is thought to mediate its function through interaction with unknown cellular factors. Here, we report the identification of the Nedd4-1ike family of E3 ubiquitin protein ligases as proteins that specifically interact with the Rous sarcoma virus (RSV) L domain in vitro and in vivo. We screened a chicken embryo cDNA expression library by using a peptide derived from the RSV p2b sequence, isolating two unique partial cDNA clones. Neither clone interacted with a peptide containing mutations known to disrupt in vivo RSV L domain function or with human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) L domain-derived peptides. The WW domain region of one of the clones, late domain-interacting protein 1 (LDI-1), but not the C2 domain, bound RSV Gag and inhibited RSV Gag budding from human 293 cells in a dominant-negative manner, functionally implicating LDI-1 in RSV particle budding from cells. RSV Gag can be coimmune precipitated from cell extracts with an antisera directed at an exogenously expressed hemagglutinin (HA)-tagged LDI-1 or endogenous Nedd4 proteins. These findings mechanistically link the cellular ubiquitination pathway to retrovirus budding.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Avian Sarcoma Viruses - genetics</subject><subject>Avian Sarcoma Viruses - metabolism</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Budding</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Chick Embryo</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>COS cells</subject><subject>DNA, Complementary</subject><subject>Endosomal Sorting Complexes Required for Transport</subject><subject>Equine infectious anemia virus</subject><subject>gag protein</subject><subject>Gene Library</subject><subject>Gene Products, gag - chemistry</subject><subject>Gene Products, gag - genetics</subject><subject>Gene Products, gag - metabolism</subject><subject>Genes, gag</subject><subject>HIV 1</subject><subject>HIV-1 - metabolism</subject><subject>Human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Infectious Anemia Virus, Equine - metabolism</subject><subject>late domain-interacting protein 1</subject><subject>Ligases - metabolism</subject><subject>Mathematical functions</subject><subject>Nedd4 protein</subject><subject>Nedd4 Ubiquitin Protein Ligases</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Rous sarcoma virus</subject><subject>Transfection</subject><subject>ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitins</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksuOEzEQRS0EYkJgywqBxQKxSfCr_ZDYQGCGkSJAA8PWcnfbiaPudsZ2A_MzfCsOCeGxgJVVrnOrXOULwH2M5hgJ-mw7mDQnCBMulZI3wAQjhWecKXQTTBAiYiYZYSfgTkobhJCqJLoNTjCuOGGCTsC39zFk64cEL2xnsm1hDjCvLXxr25bBU9P77hoGBy9rfzX67Ad4UMClX5lkEzwfso2myfCLz-sf2iV8FXpTkKK7CGOCH0xsyg385GOJzNBCE23pWCrG0tKFCM_MCr4c29YPK-hi6OHCdl26C2450yV773BOweXp64-LN7Plu7PzxYvlrKkIyrNKOqyU4pgKx6QjhgohS2Bdy5kgzCjCcF3XpsIEOScQd7WkvKUVVQ5LQqfg-b7udqx72zZ2yNF0eht9b-K1DsbrPzODX-tV-KwrKco3TMGTgzyGq9GmrHufmjKAGWyZX4vSlnKG_gtiiTFl1Q58_Be4CWMcyg50-W3KleA7aL6HmhhSitYdH4yR3tlD7-yhj_Yogoe_j_kLP_ihAE8PwE74M61kqVGgsmPtxq7L9msu6KN_o4V4sCc2KYd4RCiqOFeEfgcSrdgc</recordid><startdate>20010925</startdate><enddate>20010925</enddate><creator>Kikonyogo, Alexandra</creator><creator>Bouamr, Fadila</creator><creator>Vana, Marcy L.</creator><creator>Xiang, Yan</creator><creator>Aiyar, Ashok</creator><creator>Carter, Carol</creator><creator>Leis, Jonathan</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010925</creationdate><title>Proteins Related to the Nedd4 Family of Ubiquitin Protein Ligases Interact with the L Domain of Rous Sarcoma Virus and are Required for Gag Budding from Cells</title><author>Kikonyogo, Alexandra ; 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Here, we report the identification of the Nedd4-1ike family of E3 ubiquitin protein ligases as proteins that specifically interact with the Rous sarcoma virus (RSV) L domain in vitro and in vivo. We screened a chicken embryo cDNA expression library by using a peptide derived from the RSV p2b sequence, isolating two unique partial cDNA clones. Neither clone interacted with a peptide containing mutations known to disrupt in vivo RSV L domain function or with human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) L domain-derived peptides. The WW domain region of one of the clones, late domain-interacting protein 1 (LDI-1), but not the C2 domain, bound RSV Gag and inhibited RSV Gag budding from human 293 cells in a dominant-negative manner, functionally implicating LDI-1 in RSV particle budding from cells. RSV Gag can be coimmune precipitated from cell extracts with an antisera directed at an exogenously expressed hemagglutinin (HA)-tagged LDI-1 or endogenous Nedd4 proteins. These findings mechanistically link the cellular ubiquitination pathway to retrovirus budding.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11562473</pmid><doi>10.1073/pnas.201268998</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antibodies Avian Sarcoma Viruses - genetics Avian Sarcoma Viruses - metabolism Binding Sites Biochemistry Biological Sciences Budding Calcium-Binding Proteins - metabolism Cell Line Cell lines Cells Chick Embryo Cloning, Molecular Complementary DNA COS cells DNA, Complementary Endosomal Sorting Complexes Required for Transport Equine infectious anemia virus gag protein Gene Library Gene Products, gag - chemistry Gene Products, gag - genetics Gene Products, gag - metabolism Genes, gag HIV 1 HIV-1 - metabolism Human immunodeficiency virus 1 Humans Infectious Anemia Virus, Equine - metabolism late domain-interacting protein 1 Ligases - metabolism Mathematical functions Nedd4 protein Nedd4 Ubiquitin Protein Ligases Plasmids Proteins Recombinant Proteins - metabolism Rous sarcoma virus Transfection ubiquitin-protein ligase Ubiquitin-Protein Ligases Ubiquitins Viruses |
| title | Proteins Related to the Nedd4 Family of Ubiquitin Protein Ligases Interact with the L Domain of Rous Sarcoma Virus and are Required for Gag Budding from Cells |
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