Kaposi’s sarcoma-associated herpesvirus lana2 protein interacts with the pocket proteins and inhibits their sumoylation
Autor: | Laura Marcos-Villar, César Muñoz-Fontela, Carmen Rivas, Manuel S. Rodriguez, C F de la Cruz-Herrera, Dolores González, Michela Campagna, Pedro Gallego, Fernando Lopitz-Otsoa |
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Rok vydání: | 2013 |
Předmět: |
Cancer Research
viruses Blotting Western SUMO protein Sumoylation virus diseases Retinoblastoma-Like Protein p107 Biology medicine.disease_cause Retinoblastoma Protein Virology Viral Proteins Crk-Associated Substrate Protein Cell Line Tumor Herpesvirus 8 Human Interferon Regulatory Factors Genetics medicine Humans Immunoprecipitation Kaposi's sarcoma-associated herpesvirus Molecular Biology |
Zdroj: | Oncogene. 33:495-503 |
ISSN: | 1476-5594 0950-9232 |
Popis: | The pocket proteins retinoblastoma protein (pRb), p107 and p130 are the key targets of oncoproteins expressed by DNA tumor viruses. Some of these viral proteins contain an LXCXE motif that mediates the interaction with the three pocket proteins and the inhibition of the pRb SUMOylation. Kaposi's sarcoma herpesvirus (KSHV) contains at least two proteins that can regulate pRb function but, so far, a KSHV-encoded protein targeting p107 and p130 has not been identified. Here, we show that the KSHV latent protein LANA2 binds to pRb, p107 and p130. LANA2 contains an LXCXE motif that is required for bypassing pRb-mediated cell-cycle arrest and for inhibiting pRb SUMOylation. Finally, we demonstrate that, in addition to pRb, both p107 and p130 can be SUMOylated, and this modification is also inhibited by LANA2 in an LXCXE-dependent manner. These results demonstrate, for the first time, the SUMOylation of p107 or p130 and, so far, they represent the first example of a KSHV protein able to interact with the three pocket proteins and to inhibit their conjugation to SUMO. |
Databáze: | OpenAIRE |
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