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Perspectivas de atuação do psicólogo escolar na rede pública de ensino: um estudo exploratório em uma escola de Fortaleza <span class="so-article-trans-title" dir="auto"> Translated title: Working perspectives for a school psychologist within public schools: an exploratory study in a school in the city of Fortaleza </span> <span class="so-article-trans-title" dir="auto"> Translated title: Perspectivas de la actuación de los psicólogos escolares en el sistema de escuelas públicas: un estudio exploratorio en una escuela en Fortaleza </span>
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      Human papillomavirus immortalization and transformation functions

      Author(s): ,
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      Journal: Virus Research
      Publisher: Elsevier BV

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          Abstract

          The high risk HPVs (such as HPV-16 and HPV-18) that are associated with specific anogenital cancers encode two oncoproteins E6 and E7, which are expressed in the HPV positive cancers. The E7 protein functions in cellular transformation, at least in part, through interactions with pRB and the other pRB related 'pocket proteins'. The major target of the E6 oncoprotein encoded by the genital tract, cancer associated human papillomaviruses is p53. Several lines of evidence suggest that E6 and E7 have additional targets important to the oncogenic potential of the virus. Work from a number of laboratories has focused on determining other activities of HPV relevant to carcinogenesis and identifying additional cellular targets of E6 and E7. This paper will review the state of the field at the time of the 19th International Papillomavirus Workshop in September 2001 with respect to the HPV encoded oncoproteins.

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          Association of human papillomavirus types 16 and 18 E6 proteins with p53.

          B Werness, A J Levine, P. M. Howley (1990)
          Human papillomavirus type 16 (HPV-16) is a DNA tumor virus that is associated with human anogenital cancers and encodes two transforming proteins, E6 and E7. The E7 protein has been shown to bind to the retinoblastoma tumor suppressor gene product, pRB. This study shows that the E6 protein of HPV-16 is capable of binding to the cellular p53 protein. The ability of the E6 proteins from different human papillomaviruses to form complexes with p53 was assayed and found to correlate with the in vivo clinical behavior and the in vitro transforming activity of these different papillomaviruses. The wild-type p53 protein has tumor suppressor properties and has also been found in association with large T antigen and the E1B 55-kilodalton protein in cells transformed by SV40 and by adenovirus type 5, respectively, providing further evidence that the human papillomaviruses, the adenoviruses, and SV40 may effect similar cellular pathways in transformation.
          Article 0 comments Cited 280 times – based on 0 reviews     Review now
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            Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade.

            M Scheffner, U Nuber, J M Huibregtse (1995)
            Ubiquitination of proteins involves the concerted action of the E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzymes and E3 ubiquitin-protein ligases. It has been proposed that E3s function as 'docking proteins', specifically binding substrate proteins and specific E2s, and that ubiquitin is then transferred directly from E2s to substrates. We show here that formation of a ubiquitin thioester on E6-AP, an E3 involved in the human papillomavirus E6-induced ubiquitination of p53 (refs 6-10), is an intermediate step in E6-AP-dependent ubiquitination. The order of ubiquitin transfer is from E1 to E2, from E2 to E6-AP, and finally from E6-AP to a substrate. This cascade of ubiquitin thioester complexes suggests that E3s have a defined enzymatic activity and do not function simply as docking proteins. The cysteine residue of E6-AP responsible for ubiquitin thioester formation was mapped to a region that is highly conserved among several proteins of unknown function, suggesting that these proteins share the ability to form thioesters with ubiquitin.
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              Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade.

              L. Huang, P Howley, G Wang … (1999)
              The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3.
              Article 0 comments Cited 147 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Title: Virus Research
                Abbreviated Title: Virus Research
                Publisher: Elsevier BV
                ISSN (Print): 01681702
                Publication date Created: November 2002
                Publication date (Print): November 2002
                Volume: 89
                Issue: 2
                Pages: 213-228
                Article
                DOI: 10.1016/S0168-1702(02)00190-9
                PubMed ID: 12445661
                SO-VID: 456b734c-6432-4b63-a01b-2f8b49148fdc
                Copyright © © 2002
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                https://www.elsevier.com/tdm/userlicense/1.0/

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