ArticleJournal of virology2005
Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- SAMHD1 enhances HIV-1-induced apoptosis in monocytic cells via the mitochondrial pathway.mBio · 2025Article
- Virus-Host Protein Interaction Network of the Hepatitis E Virus ORF2-4 by Mammalian Two-Hybrid Assays.Viruses · 2023Article
- Zooming into the structure-function of RING finger proteins for anti-cancer therapeutic applications.American journal of cancer research · 2023Review
- The Role of E3 Ligase Pirh2 in Disease.Cells · 2022Review
- Links between Infections, Lung Cancer, and the Immune System.International journal of molecular sciences · 2021Review
- The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the Phosphoprotein.Journal of virology · 2020Article
- Regulation of measles virus gene expression by P protein coiled-coil properties.Science advances · 2019Article
- A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation.Journal of virology · 2018Article
- Relevance of the Measles Virus Expression in Cancer - an Update.Pathology oncology research : POR · 2016Review
- p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- HSP90 Chaperoning in Addition to Phosphoprotein Required for Folding but Not for Supporting Enzymatic Activities of Measles and Nipah Virus L Polymerases.Journal of virology · 2016Article
- Sequence of events in measles virus replication: role of phosphoprotein-nucleocapsid interactions.Journal of virology · 2014Article
- RIG-I self-oligomerization is either dispensable or very transient for signal transduction.PloS one · 2014Article
- Does the measles virus contribute to carcinogenesis? - a review.Journal of Cancer · 2014Review
- Article
- Pirh2 RING-finger E3 ubiquitin ligase: its role in tumorigenesis and cancer therapy.FEBS letters · 2012Review
- A novel oncoprotein Pirh2: rising from the shadow of MDM2.Cancer science · 2011Review
- The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment.Virology journal · 2009Article
- Refined study of the interaction between HIV-1 p6 late domain and ALIX.Retrovirology · 2008Article
- Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA.Journal of virology · 2007Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using a C-terminal domain (PCT) of the measles virus (MV) phosphoprotein (P protein) as bait in a yeast two-hybrid screen, a cDNA identical to the recently described human p53-induced-RING-H2 (hPIRH2) cDNA was isolated. A glutathione S-transferase-hPIRH2 fusion protein expressed in bacteria was able to pull down P protein when mixed with an extract from P-expressing HeLa cells in vitro, and myc-tagged hPIRH2 could be reciprocally co-immunoprecipitated with MV P protein from human cells. Additionally, immunoprecipitation experiments demonstrated that hPIRH2-myc, MV P, and nucleocapsid (N) proteins form a ternary complex. The hPIRH2 binding site was mapped to the C-terminal X domain region of the P protein by using a yeast two-hybrid assay. The PCT binding site was mapped on hPIRH2 by using a novel yeast two-hybrid tagged PCR approach and by co-immunoprecipitation of hPIRH2 cysteine mutants and mouse/human PIRH2 chimeras. The hPIRH2 C terminus could mediate the interaction with MV P which was favored by the RING-H2 motif. When coexpressed with an enhanced green fluorescent protein-tagged hPIRH2 protein, MV P alone or in a complex with MV N was able to redistribute hPIRH2 to outside the nucleus, within intracellular aggregates. Finally, MV P efficiently stabilized hPIRH2-myc expression and prevented its ubiquitination in vivo but had no effect on the stability or ubiquitination of an alternative ubiquitin E3 ligase, Mdm2. Thus, MV P protein is the first protein from a pathogen that is able to specifically interact with and stabilize the ubiquitin E3 ligase hPIRH2 by preventing its ubiquitination.
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