ArticleProceedings of the National Academy of Sciences of the United States of America1997
Multiple protein domains determine the cell type-specific nuclear distribution of the catalytic subunit required for apolipoprotein B mRNA editing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
- Review
- Review
- Opossum APOBEC1 is a DNA mutator with retrovirus and retroelement restriction activity.Scientific reports · 2017Article
- The APOBEC Protein Family: United by Structure, Divergent in Function.Trends in biochemical sciences · 2016Review
- Creation of chimeric human/rabbit APOBEC1 with HIV-1 restriction and DNA mutation activities.Scientific reports · 2016Article
- Flow-cytometric visualization of C>U mRNA editing reveals the dynamics of the process in live cells.RNA biology · 2015Article
- The role of cytidine deaminases on innate immune responses against human viral infections.BioMed research international · 2013Review
- APOBEC3B and AID have similar nuclear import mechanisms.Journal of molecular biology · 2012Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
- Intrinsic restriction activity by apolipoprotein B mRNA editing enzyme APOBEC1 against the mobility of autonomous retrotransposons.Nucleic acids research · 2011Article
- Active nuclear import and cytoplasmic retention of activation-induced deaminase.Nature structural & molecular biology · 2009Article
- Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.Journal of virology · 2008Article
- The AID/APOBEC family of nucleic acid mutators.Genome biology · 2008Review
- Functional characterization of APOBEC-1 complementation factor phosphorylation sites.Biochimica et biophysica acta · 2007Article
- C to U editing at position 32 of the anticodon loop precedes tRNA 5' leader removal in trypanosomatids.Nucleic acids research · 2007Article
- APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic.Biochemical and biophysical research communications · 2006Article
- Metabolic regulation of apoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor.Nucleic acids research · 2006Article
- Targeted deletion of the murine apobec-1 complementation factor (acf) gene results in embryonic lethality.Molecular and cellular biology · 2005Article
- Somatic hypermutation is limited by CRM1-dependent nuclear export of activation-induced deaminase.The Journal of experimental medicine · 2004Article
- Activation-induced cytidine deaminase shuttles between nucleus and cytoplasm like apolipoprotein B mRNA editing catalytic polypeptide 1.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein B (apoB) mRNA editing catalyzed by apoB mRNA editing catalytic subunit 1 (APOBEC-1) has been proposed to be a nuclear process. To test this hypothesis, the subcellular distribution of hemagglutinin- (HA) tagged APOBEC-1 expressed in transiently transfected hepatoma cells was determined by indirect immunofluorescence microscopy. HA-APOBEC-1 was detected in both the nucleus and cytoplasm of rat and human hepatoma cells. Mutagenesis of APOBEC-1 demonstrated that the N-terminal 56 amino acids (1-56) were necessary for the nuclear distribution of APOBEC-1, but this region did not contain a functional nuclear localization signal (NLS). However, we identified a 24-amino acid domain in the C terminus of APOBEC-1 with characteristics of a cytoplasmic retention signal (CRS) or a nuclear export signal (NES). These data suggest, therefore, that the nuclear import of APOBEC-1 may not be mediated by a positive NLS; rather, it may be achieved by overcoming the effect of a CRS/NES. We also demonstrated that the nuclear distribution of APOBEC-1 occurred only in cell lines that were capable of editing apoB RNA. We propose that the cellular distribution of APOBEC-1 is determined by multiple domains within this protein, and a nuclear localization of the enzyme may be regulated by cell type-specific factors that render these cells uniquely editing competent.
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