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Functional characterization of APOBEC-1 complementation factor phosphorylation sites.

David M Lehmann1, Chad A Galloway, Celeste MacElrevey

  • 1Environmental Health Sciences Center, Department of Toxicology, University of Rochester, Rochester, NY 14642, USA.

Biochimica Et Biophysica Acta
|January 19, 2007
PubMed
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Protein kinase C (PKC) activates apolipoprotein B (ApoB) mRNA editing by phosphorylating the APOBEC-1 complementation factor (ACF). This phosphorylation is crucial for metabolic regulation of ApoB mRNA editing in liver cells.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Gene Regulation

Background:

  • Apolipoprotein B (ApoB) mRNA editing is a critical post-transcriptional modification in hepatocytes.
  • This process requires apolipoprotein B mRNA editing catalytic subunit 1 (APOBEC-1) and apolipoprotein B mRNA editing factor (ACF).
  • Metabolic regulation of ApoB mRNA editing is linked to ACF phosphorylation within nuclear editosomes.

Purpose of the Study:

  • To investigate the role of protein kinases in the metabolic regulation of ApoB mRNA editing.
  • To determine if protein kinase C (PKC) or protein kinase A (PKA) influences ACF phosphorylation and ApoB mRNA editing.
  • To elucidate the specific phosphorylation sites on ACF involved in metabolic regulation.

Main Methods:

  • Treatment of rat primary hepatocytes with PKC and PKA activators.

Related Experiment Videos

  • Assessment of ApoB mRNA editing activity and ACF phosphorylation levels.
  • In vitro phosphorylation assays using purified ACF64 and recombinant kinases.
  • Site-directed mutagenesis of predicted PKC phosphorylation sites (S154, S368) on ACF.

    • Main Results:

    • PKC activation significantly stimulated ApoB mRNA editing and ACF phosphorylation in hepatocytes.
    • PKA activation had no discernible effect on ApoB mRNA editing or ACF phosphorylation.
    • Recombinant PKC phosphorylated ACF64 in vitro, while PKA did not.
    • Mutating PKC sites S154 and S368 to alanine abolished ethanol-induced editing, while aspartic acid substitution mimicked ethanol treatment.

    Conclusions:

    • PKC-mediated phosphorylation of ACF at sites S154 and S368 is a key regulatory mechanism for ApoB mRNA editing.
    • This phosphorylation pathway is involved in the metabolic control of ApoB mRNA editing in rat hepatocytes.
    • The findings highlight a specific molecular mechanism linking cellular metabolism to gene expression regulation.