ArticleRetrovirology2012
Identification and characterization of naturally occurring splice variants of SAMHD1.
Article in Retrovirology, 2012. 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, 32 citations in OpenAlex.
- Article
- SAMHD1 single nucleotide polymorphisms impact outcome in children with newly diagnosed acute myeloid leukemia.Blood advances · 2023Article
- Dual roles of SAMHD1 in tumor development and chemoresistance to anticancer drugs.Oncology letters · 2021Review
- Conserved Herpesvirus Protein Kinases Target SAMHD1 to Facilitate Virus Replication.Cell reports · 2019Article
- Profiling of LINE-1-Related Genes in Hepatocellular Carcinoma.International journal of molecular sciences · 2019Review
- SAMHD1: Recurring roles in cell cycle, viral restriction, cancer, and innate immunity.Autoimmunity · 2018Review
- Mannose Receptor 1 Restricts HIV Particle Release from Infected Macrophages.Cell reports · 2018Article
- CD81 association with SAMHD1 enhances HIV-1 reverse transcription by increasing dNTP levels.Nature microbiology · 2017Article
- Low dNTP levels are necessary but may not be sufficient for lentiviral restriction by SAMHD1.Virology · 2016Article
- Immunogenetics of systemic lupus erythematosus: A comprehensive review.Journal of autoimmunity · 2015Review
- Incorporating alternative splicing and mRNA editing into the genetic analysis of complex traits.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014Article
- SAMHD1 has differential impact on the efficacies of HIV nucleoside reverse transcriptase inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- The genetic basis for individual differences in mRNA splicing and APOBEC1 editing activity in murine macrophages.Genome research · 2014Article
- HIV accessory proteins versus host restriction factors.Current opinion in virology · 2013Review
- Restriction of virus infection but not catalytic dNTPase activity is regulated by phosphorylation of SAMHD1.Journal of virology · 2013Article
- Host Factors and HIV-1 Replication: Clinical Evidence and Potential Therapeutic Approaches.Frontiers in immunology · 2013Review
- Cellular and Biochemical Mechanisms of the Retroviral Restriction Factor SAMHD1.ISRN biochemistry · 2013Article
- Promoter methylation regulates SAMHD1 gene expression in human CD4+ T cells.The Journal of biological chemistry · 2013Article
- Interferon block to HIV-1 transduction in macrophages despite SAMHD1 degradation and high deoxynucleoside triphosphates supply.Retrovirology · 2013Article
- Host restriction factors in retroviral infection: promises in virus-host interaction.Retrovirology · 2012Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundSterile Alpha Motif and HD domain-containing protein 1 (SAMHD1) is a recently identified host factor that restricts HIV-1 replication in dendritic and myeloid cells. SAMHD1 is a dNTPase that presumably reduces the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. However, HIV-2 and SIV encoded Vpx counteracts the antiviral effects of SAMHD1 by targeting the protein for proteasomal degradation. SAMHD1 is encoded by a multiply spliced mRNA and consists of 16 coding exons.
resultsHere, we identified two naturally occurring splice variants lacking exons 8-9 and 14, respectively. Like wildtype SAMHD1, both splice variants localize primarily to the nucleus, interact with Vpx, and retain some sensitivity to Vpx-dependent degradation. However, the splice variants differ from full-length SAMHD1 in their metabolic stability and catalytic activity. While full-length SAMHD1 is metabolically stable in uninfected cells, both splice variants were inherently metabolically unstable and were rapidly degraded even in the absence of Vpx. Vpx strongly increased the rate of degradation of full-length SAMHD1 and further accelerated the degradation of the splice variants. However, the effect of Vpx on the splice variants was more modest due to the inherent instability of these proteins. Analysis of dNTPase activity indicates that neither splice variant is catalytically active.
conclusionsThe identification of SAMHD1 splice variants exposes a potential regulatory mechanism that could enable the cell to control its dNTPase activity on a post-transcriptional level.
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Registered trials
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