ArticleNucleic acids research2006
Metabolic regulation of apoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Cellular APOBEC3A deaminase drives mutations in the SARS-CoV-2 genome.Nucleic acids research · 2023Article
- Peroxisome-Deficiency and HIF-2α Signaling Are Negative Regulators of Ketohexokinase Expression.Frontiers in cell and developmental biology · 2020Article
- Apobec1 complementation factor (A1CF) and RBM47 interact in tissue-specific regulation of C to U RNA editing in mouse intestine and liver.RNA (New York, N.Y.) · 2019Article
- Review
- Review
- Flow-cytometric visualization of C>U mRNA editing reveals the dynamics of the process in live cells.RNA biology · 2015Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
- Mouse and other rodent models of C to U RNA editing.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Metabolic regulation of APOBEC-1 complementation factor trafficking in mouse models of obesity and its positive correlation with the expression of ApoB protein in hepatocytes.Biochimica et biophysica acta · 2010Article
- APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers.Biochemical and biophysical research communications · 2010Article
- The expression of apoB mRNA editing factors is not the sole determinant for the induction of editing in differentiating Caco-2 cells.Biochemical and biophysical research communications · 2010Article
- Identification of mRNA binding proteins that regulate the stability of LDL receptor mRNA through AU-rich elements.Journal of lipid research · 2009Article
- 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-mediated RNA editing.Wiley interdisciplinary reviews. Systems biology and medicineReview
- The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein B (apoB) mRNA editing is a nuclear event that minimally requires the RNA substrate, APOBEC-1 and APOBEC-1 Complementation Factor (ACF). The co-localization of these macro-molecules within the nucleus and the modulation of hepatic apoB mRNA editing activity have been described following a variety of metabolic perturbations, but the mechanism that regulates editosome assembly is unknown. APOBEC-1 was effectively co-immunoprecipitated with ACF from nuclear, but not cytoplasmic extracts. Moreover, alkaline phosphatase treatment of nuclear extracts reduced the amount of APOBEC-1 co-immunoprecipitated with ACF and inhibited in vitro editing activity. Ethanol stimulated apoB mRNA editing was associated with a 2- to 3-fold increase in ACF phosphorylation relative to that in control primary hepatocytes. Significantly, phosphorylated ACF was restricted to nuclear extracts where it co-sedimented with 27S editing competent complexes. Two-dimensional phosphoamino acid analysis of ACF immunopurified from hepatocyte nuclear extracts demonstrated phosphorylation of serine residues that was increased by ethanol treatment. Inhibition of protein phosphatase I, but not PPIIA or IIB, stimulated apoB mRNA editing activity coincident with enhanced ACF phosphorylation in vivo. These data demonstrate that ACF is a metabolically regulated phosphoprotein and suggest that this post-translational modification increases hepatic apoB mRNA editing activity by enhancing ACF nuclear localization/retention, facilitating the interaction of ACF with APOBEC-1 and thereby increasing the probability of editosome assembly and activity.
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