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Oncogene v.37 no.21, 2018년, pp.2806 - 2816   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Stability of HTLV-2 antisense protein is controlled by PML nuclear bodies in a SUMO-dependent manner

Dubuisson, Louise (International Center for Research in Infectiology, Retroviral Oncogenesis Laboratory, INSERM U1111 – ) ; Lormières, Florence (Université ) ; Fochi, Stefania (Claude Bernard Lyon 1, CNRS, UMR5308, Ecole Normale Supérieure de Lyon, Université ) ; Turpin, Jocelyn (Lyon, F-69007, Lyon, France ) ; Pasquier, Amandine (Equipe labellisée “Ligue Nationale Contre le Cancer”, Lyon, France ) ; Douceron, Estelle (International Center for Research in Infectiology, Retroviral Oncogenesis Laboratory, INSERM U1111 – ) ; Oliva, Anaïs (Université ) ; Bazarbachi, Ali (Claude Bernard Lyon 1, CNRS, UMR5308, Ecole Normale Supérieure de Lyon, Université ) ; Lallemand-Breitenbach, Valérie (Lyon, F-69007, Lyon, France ) ; De Thé, Hugues (Equipe labellisée “Ligue Nationale Contre le Cancer”, Lyon, France ) ; Journo, Chloé (Department of Neurosciences, Biomedicine and Movement Sciences, University of Verona, Verona, Italy ) ; Mahieux, Renaud (International Center for Research in Infectiology, Retroviral Oncogenesis Laboratory, INSERM U1111 – ) ;
  • 초록  

    Since the identification of the antisense protein of HTLV-2 (APH-2) and the demonstration that APH-2 mRNA is expressed in vivo in most HTLV-2 carriers, much effort has been dedicated to the elucidation of similarities and/or differences between APH-2 and HBZ, the antisense protein of HTLV-1. Similar to HBZ, APH-2 negatively regulates HTLV-2 transcription. However, it does not promote cell proliferation. In contrast to HBZ, APH-2 half-life is very short. Here, we show that APH-2 is addressed to PML nuclear bodies in T-cells, as well as in different cell types. Covalent SUMOylation of APH-2 is readily detected, indicating that APH-2 might be addressed to the PML nuclear bodies in a SUMO-dependent manner. We further show that silencing of PML increases expression of APH-2, while expression of HBZ is unaffected. On the other hand, SUMO-1 overexpression leads to a specific loss of APH-2 expression that is restored upon proteasome inhibition. Furthermore, the carboxy-terminal LAGLL motif of APH-2 is responsible for both the targeting of the protein to PML nuclear bodies and its short half-life. Taken together, these observations indicate that natural APH-2 targeting to PML nuclear bodies induces proteasomal degradation of the viral protein in a SUMO-dependent manner. Hence, this study deciphers the molecular and cellular bases of APH-2 short half-life in comparison to HBZ and highlights key differences in the post-translational mechanisms that control the expression of both proteins.


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