Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing
The editing of apolipoprotein B (apoB) mRNA is under tissue-specific, developmental and metabolic regulation. We found that multiple protein kinase inhibitors or activators increased apoB mRNA editing up to 2.5-fold in Caco-2 cells and 3–8-fold in McA7777 and FAO rat cells respectively. The phosphor...
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crportlandpress:10.1042/bj3570661 2024-04-07T07:51:47+00:00 Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing CHEN, Zhigang EGGERMAN, Thomas L. PATTERSON, Amy P. 2001 http://dx.doi.org/10.1042/bj3570661 https://portlandpress.com/biochemj/article-pdf/357/3/661/708041/bj3570661.pdf en eng Portland Press Ltd. Biochemical Journal volume 357, issue 3, page 661-672 ISSN 0264-6021 1470-8728 Cell Biology Molecular Biology Biochemistry journal-article 2001 crportlandpress https://doi.org/10.1042/bj3570661 2024-03-08T03:11:37Z The editing of apolipoprotein B (apoB) mRNA is under tissue-specific, developmental and metabolic regulation. We found that multiple protein kinase inhibitors or activators increased apoB mRNA editing up to 2.5-fold in Caco-2 cells and 3–8-fold in McA7777 and FAO rat cells respectively. The phosphorylation-agent-induced modulation is independent of the apolipoprotein B editing catalytic subunit 1 (APOBEC-1) and of apoB mRNA expression levels, indicating the involvement of a protein modification, such as phosphorylation, regulating the cellular editing of apoB mRNA. Transient expression of protein kinase C-θ more than doubled apoB mRNA editing in FAO cells. Chronic exposure to ethanol, a treatment known to increase the expression of protein kinases and to change protein phosphorylation status, increased apoB mRNA editing in FAO cells up to 2.5-fold without increasing the mRNA abundance of APOBEC-1. The elimination of potential phosphorylation sites 47 and 72 of human APOBEC-1 decreased its activity to approx. one-eighth of control levels by a Ser47 → Ala mutation, but more than doubled the activity by a Ser72 → Ala mutation. The activity modulation was reversed by a Ser → Asp mutation at sites 47 and 72, which introduced a phosphorylation-like carbonic acid group. Both human APOBEC-1 dephosphorylated by alkaline phosphase and the Ser47,72-to-alanine double mutant protein demonstrated a shifted isoelectric focusing pattern compared with the wild type, indicating phosphorylation at these sites. Taken together, these results suggest that phosphorylation might be an important mechanism in the regulation of apoB mRNA editing. Article in Journal/Newspaper Carbonic acid Portland Press Biochemical Journal 357 3 661 672 |
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Portland Press |
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English |
topic |
Cell Biology Molecular Biology Biochemistry |
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Cell Biology Molecular Biology Biochemistry CHEN, Zhigang EGGERMAN, Thomas L. PATTERSON, Amy P. Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
The editing of apolipoprotein B (apoB) mRNA is under tissue-specific, developmental and metabolic regulation. We found that multiple protein kinase inhibitors or activators increased apoB mRNA editing up to 2.5-fold in Caco-2 cells and 3–8-fold in McA7777 and FAO rat cells respectively. The phosphorylation-agent-induced modulation is independent of the apolipoprotein B editing catalytic subunit 1 (APOBEC-1) and of apoB mRNA expression levels, indicating the involvement of a protein modification, such as phosphorylation, regulating the cellular editing of apoB mRNA. Transient expression of protein kinase C-θ more than doubled apoB mRNA editing in FAO cells. Chronic exposure to ethanol, a treatment known to increase the expression of protein kinases and to change protein phosphorylation status, increased apoB mRNA editing in FAO cells up to 2.5-fold without increasing the mRNA abundance of APOBEC-1. The elimination of potential phosphorylation sites 47 and 72 of human APOBEC-1 decreased its activity to approx. one-eighth of control levels by a Ser47 → Ala mutation, but more than doubled the activity by a Ser72 → Ala mutation. The activity modulation was reversed by a Ser → Asp mutation at sites 47 and 72, which introduced a phosphorylation-like carbonic acid group. Both human APOBEC-1 dephosphorylated by alkaline phosphase and the Ser47,72-to-alanine double mutant protein demonstrated a shifted isoelectric focusing pattern compared with the wild type, indicating phosphorylation at these sites. Taken together, these results suggest that phosphorylation might be an important mechanism in the regulation of apoB mRNA editing. |
format |
Article in Journal/Newspaper |
author |
CHEN, Zhigang EGGERMAN, Thomas L. PATTERSON, Amy P. |
author_facet |
CHEN, Zhigang EGGERMAN, Thomas L. PATTERSON, Amy P. |
author_sort |
CHEN, Zhigang |
title |
Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
title_short |
Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
title_full |
Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
title_fullStr |
Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
title_full_unstemmed |
Phosphorylation is a regulatory mechanism in apolipoprotein B mRNA editing |
title_sort |
phosphorylation is a regulatory mechanism in apolipoprotein b mrna editing |
publisher |
Portland Press Ltd. |
publishDate |
2001 |
url |
http://dx.doi.org/10.1042/bj3570661 https://portlandpress.com/biochemj/article-pdf/357/3/661/708041/bj3570661.pdf |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_source |
Biochemical Journal volume 357, issue 3, page 661-672 ISSN 0264-6021 1470-8728 |
op_doi |
https://doi.org/10.1042/bj3570661 |
container_title |
Biochemical Journal |
container_volume |
357 |
container_issue |
3 |
container_start_page |
661 |
op_container_end_page |
672 |
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1795666873107349504 |