Papillomavirus E6 oncoproteins
Identifieur interne : 000104 ( Pmc/Curation ); précédent : 000103; suivant : 000105Papillomavirus E6 oncoproteins
Auteurs : Scott B. Vande Pol ; Aloysius J. Klingelhutz [États-Unis]Source :
- Virology [ 0042-6822 ] ; 2013.
Abstract
Papillomaviruses induce benign and malignant epithelial tumors, and the viral E6 oncoprotein is essential for full transformation. E6 contributes to transformation by associating with cellular proteins, docking on specific acidic LXXLL peptide motifs found on the associated cellular proteins. This review examines insights from recent studies of human and animal E6 proteins that determine the three-dimensional structure of E6 when bound to acidic LXXLL peptides. The structure of E6 is related to recent advances in the purification and identification of E6 associated protein complexes. These E6 protein-complexes, together with other proteins that bind to E6, alter a broad array of biological outcomes including modulation of cell survival, cellular transcription, host cell differentiation, growth factor dependence, DNA damage responses, and cell cycle progression.
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DOI: 10.1016/j.virol.2013.04.026
PubMed: 23711382
PubMed Central: 3783570
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Scott B. Vande Pol<affiliation><nlm:aff id="A1">Department of Pathology, University of Virginia, Charlottesville, Virginia. 22901</nlm:aff><wicri:noCountry code="subfield">Virginia. 22901</wicri:noCountry></affiliation>Le document en format XML
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0110674</journal-id><journal-id journal-id-type="pubmed-jr-id">8015</journal-id><journal-id journal-id-type="nlm-ta">Virology</journal-id><journal-id journal-id-type="iso-abbrev">Virology</journal-id><journal-title-group><journal-title>Virology</journal-title></journal-title-group><issn pub-type="ppub">0042-6822</issn><issn pub-type="epub">1096-0341</issn></journal-meta><article-meta><article-id pub-id-type="pmid">23711382</article-id><article-id pub-id-type="pmc">3783570</article-id><article-id pub-id-type="doi">10.1016/j.virol.2013.04.026</article-id><article-id pub-id-type="manuscript">NIHMS485569</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Papillomavirus E6 oncoproteins</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Vande Pol</surname><given-names>Scott B.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref rid="FN1" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Klingelhutz</surname><given-names>Aloysius J.</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib></contrib-group><aff id="A1"><label>1</label>Department of Pathology, University of Virginia, Charlottesville, Virginia. 22901</aff><aff id="A2"><label>2</label>Department of Microbiology, University of Iowa. Iowa City, Iowa 52242</aff><author-notes><corresp id="FN1"><label>*</label>Address correspondence to: Dr. Scott Vande Pol, Department of Pathology, University of Virginia, P.O. Box 800904, Charlottesville, VA 22908-0904. <email>vandepol@virginia.edu</email>; Phone 434-924-1603; Fax 434-924-2151</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>17</day><month>6</month><year>2013</year></pub-date><pub-date pub-type="epub"><day>24</day><month>5</month><year>2013</year></pub-date><pub-date pub-type="ppub"><month>10</month><year>2013</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>10</month><year>2014</year></pub-date><volume>445</volume><issue>0</issue><fpage>115</fpage><lpage>137</lpage><permissions><copyright-statement>© 2013 Elsevier Inc. All rights reserved.</copyright-statement><copyright-year>2013</copyright-year></permissions><abstract><p id="P2">Papillomaviruses induce benign and malignant epithelial tumors, and the viral E6 oncoprotein is essential for full transformation. E6 contributes to transformation by associating with cellular proteins, docking on specific acidic LXXLL peptide motifs found on the associated cellular proteins. This review examines insights from recent studies of human and animal E6 proteins that determine the three-dimensional structure of E6 when bound to acidic LXXLL peptides. The structure of E6 is related to recent advances in the purification and identification of E6 associated protein complexes. These E6 protein-complexes, together with other proteins that bind to E6, alter a broad array of biological outcomes including modulation of cell survival, cellular transcription, host cell differentiation, growth factor dependence, DNA damage responses, and cell cycle progression.</p></abstract><funding-group><award-group><funding-source country="United States">National Institute of Dental and Craniofacial Research : NIDCR</funding-source><award-id>R21 DE019953 || DE</award-id></award-group><award-group><funding-source country="United States">National Cancer Institute : NCI</funding-source><award-id>R01 CA134737 || CA</award-id></award-group><award-group><funding-source country="United States">National Cancer Institute : NCI</funding-source><award-id>R01 CA120352 || CA</award-id></award-group><award-group><funding-source country="United States">National Institute on Aging : NIA</funding-source><award-id>R01 AG027388 || AG</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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