ArticleThe Journal of biological chemistry2012
Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization.PLoS pathogens · 2023Article
- The HIV-1 Integrase C-Terminal Domain Induces TAR RNA Structural Changes Promoting Tat Binding.International journal of molecular sciences · 2022Article
- Complex Relationships between HIV-1 Integrase and Its Cellular Partners.International journal of molecular sciences · 2022Review
- Review
- Natural Occurring Polymorphisms in HIV-1 Integrase and RNase H Regulate Viral Release and Autoprocessing.Journal of virology · 2021Article
- CRISPR/Cas9-Induced Mutagenesis Corroborates the Role of Transportin-SR2 in HIV-1 Nuclear Import.Microbiology spectrum · 2021Article
- Role of Transportin-SR2 in HIV-1 Nuclear Import.Viruses · 2021Review
- Integrase-RNA interactions underscore the critical role of integrase in HIV-1 virion morphogenesis.eLife · 2020Article
- TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain.Journal of virology · 2020Article
- Inhibitors of the integrase-transportin-SR2 interaction block HIV nuclear import.Retrovirology · 2018Article
- N-terminal half of transportin SR2 interacts with HIV integrase.The Journal of biological chemistry · 2017Article
- Development and validation of a cell-based assay system to assess human immunodeficiency virus type 1 integrase multimerization.Journal of virological methods · 2016Article
- HIV-1 capsid: the multifaceted key player in HIV-1 infection.Nature reviews. Microbiology · 2015Review
- Uneven genetic robustness of HIV-1 integrase.Journal of virology · 2015Article
- Comparison Between Several Integrase-defective Lentiviral Vectors Reveals Increased Integration of an HIV Vector Bearing a D167H Mutant.Molecular therapy. Nucleic acids · 2014Article
- The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.The Journal of biological chemistry · 2014Article
- Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.Viruses · 2013Review
- Interaction of transportin-SR2 with Ras-related nuclear protein (Ran) GTPase.The Journal of biological chemistry · 2013Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transportin-SR2 (TRN-SR2 and TNPO3) is a cellular cofactor of HIV replication that has been implicated in the nuclear import of HIV. TRN-SR2 was originally identified in a yeast two-hybrid screen as an interaction partner of HIV integrase (IN) and in two independent siRNA screens as a cofactor of viral replication. We have now studied the interaction of TRN-SR2 and HIV IN in molecular detail and identified the TRN-SR2 interacting regions of IN. A weak interaction with the catalytic core domain (CCD) and a strong interaction with the C-terminal domain (CTD) of IN were detected. By dissecting the catalytic core domain (CCD) of IN into short structural fragments, we identified a peptide (INIP(1), amino acids (170)EHLKTAVQMAVFIHNFKRKGGI(191)) retaining the ability to interact with TRN-SR2. By dissecting the C-terminal domain (CTD) of IN, we could identify two interacting peptides (amino acids (214)QKQITKIQNFRVYYR(228) and (262)RRKVKIIRDYGK(273)) that come together in the CTD tertiary structure to form an exposed antiparallel β-sheet. Through site-specific mutagenesis, we defined the following sets of amino acids in IN as important for the interaction with TRN-SR2: Phe-185/Lys-186/Arg-187/Lys-188 in the CCD and Arg-262/Arg-263/Lys-264 and Lys-266/Arg-269 in the CTD. An HIV-1 strain carrying K266A/R269A in IN was replication-defective due to a block in reverse transcription, confounding the study of nuclear import. Insight into the IN/TRN-SR2 interaction interface is necessary to guide drug discovery efforts targeting the nuclear entry step of replication.
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