Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2017 Jan 2;14(1):11-14.
doi: 10.1080/15476286.2016.1251540. Epub 2016 Oct 28.

Regulation of mRNA capping in the cell cycle

Michael Aregger  1 , Victoria H Cowling  1
Affiliations
Review

Regulation of mRNA capping in the cell cycle

Michael Aregger et al. RNA Biol. .

Abstract

The mRNA cap structure, which is added to nascent RNA pol II transcripts, recruits the protein complexes required for pre-mRNA transcript processing, mRNA export and translation initiation. The enzymes which catalyze mRNA cap synthesis are regulated by cellular signaling pathways which impact on their expression, localization and activity. Here we discuss the recent observation that the mRNA cap methyltransferase, RNMT, is phosphorylated on Thr-77 by CDK1-cyclin B1, which regulates its activity and the proteins with which it interacts. RNMT Thr-77 phosphorylation provides a burst of mRNA cap methyltransferase activity during early G1 phase at a time when transcription is reactivated following completion of the cell cycle. This co-ordination of transcription and mRNA capping makes an important contribution to gene expression in the cell; preventing RNMT Thr-77 phosphorylation inhibits cell proliferation. Here we discuss these findings and how mRNA cap synthesis may be regulated in other scenarios.

Keywords: Cell cycle; RNMT; gene expression; mRNA; mRNA cap; phosphorylation; transcription; translation.

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
mRNA cap structure and mRNA capping enzymes. Structure of mRNA cap and action of mRNA capping enzymes.
Figure 2.
Figure 2.
Post-translational modifications of RNMT. Human RNMT 1-120 is the N-terminal domain and RNMT 121-476 is the catalytic domain and interacts with RAM. Above depiction of RNMT are phosphorylation sites (P) obtained from PhosphositePlus (sites with only 1 mass spectrometry/high-throughput proteomics reference excluded). Below depiction of RNMT are phosphorylation, acetylation (Ac) and methylation (Me) sites identified from analysis in Aregger et al., 2016.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Shuman S. RNA capping: progress and prospects. Rna 2015; 21:735-7; PMID:25780214; http://dx.doi.org/10.1261/rna.049973.115 - DOI - PMC - PubMed
    1. Shatkin AJ. Capping of eucaryotic mRNAs. Cell 1976; 9:645-53; PMID:1017010; http://dx.doi.org/10.1016/0092-8674(76)90128-8 - DOI - PubMed
    1. Furuichi Y. Discovery of m(7)G-cap in eukaryotic mRNAs. Proc Jpn Acad Ser B Phys Biol Sci 2015; 91:394-409; PMID:26460318; http://dx.doi.org/10.2183/pjab.91.394 - DOI - PMC - PubMed
    1. Ramanathan A, Robb GB, Chan SH. mRNA capping: biological functions and applications. Nucleic Acids Res 2016; 44(16):7511-26; PMID:27317694; http://dx.doi.org/2195701010.1093/nar/gkw551 - DOI - PMC - PubMed
    1. Topisirovic I, Svitkin YV, Sonenberg N, Shatkin AJ. Cap and cap-binding proteins in the control of gene expression. Wiley Interdiscip Rev RNA 2011; 2:277-98; PMID:21957010; http://dx.doi.org/10.1002/wrna.52 - DOI - PubMed

Publication types

LinkOut - more resources