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Review
. 2017:963:15-33.
doi: 10.1007/978-3-319-50044-7_2.

Roles of Sumoylation in mRNA Processing and Metabolism

Patricia Richard  1 , Vasupradha Vethantham  1 , James L Manley  2
Affiliations
Review

Roles of Sumoylation in mRNA Processing and Metabolism

Patricia Richard et al. Adv Exp Med Biol. 2017.

Abstract

SUMO has gained prominence as a regulator in a number of cellular processes. The roles of sumoylation in RNA metabolism, however, while considerable, remain less well understood. In this chapter we have assembled data from proteomic analyses, localization studies and key functional studies to extend SUMO's role to the area of mRNA processing and metabolism. Proteomic analyses have identified multiple putative sumoylation targets in complexes functioning in almost all aspects of mRNA metabolism, including capping, splicing and polyadenylation of mRNA precursors. Possible regulatory roles for SUMO have emerged in pre-mRNA 3' processing, where SUMO influences the functions of polyadenylation factors and activity of the entire complex. SUMO is also involved in regulating RNA editing and RNA binding by hnRNP proteins, and recent reports have suggested the involvement of the SUMO pathway in mRNA export. Together, these reports suggest that SUMO is involved in regulation of many aspects of mRNA metabolism and hold the promise for exciting future studies.

Keywords: 3’-end processing; Capping; RNA editing; Splicing; Transcription; mRNA.

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References

    1. Barnard DC, Ryan K, Manley JL, Richter JD. Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation. Cell. 2004;119:641–651. - PubMed
    1. Becker J, Barysch SV, Karaca S, Dittner C, Hsiao HH, Berriel Diaz M, Herzig S, Urlaub H, Melchior F. Detecting endogenous SUMO targets in mammalian cells and tissues. Nat Struct Mol Biol. 2013;20:525–531. - PubMed
    1. Bellare P, Small EC, Huang X, Wohlschlegel JA, Staley JP, Sontheimer EJ. A role for ubiquitin in the spliceosome assembly pathway. Nat Struct Mol Biol. 2008;15:444–451. - PMC - PubMed
    1. Bennett CL, Chen Y, Vignali M, Lo RS, Mason AG, Unal A, Huq Saifee NP, Fields S, La Spada AR. Protein interaction analysis of senataxin and the ALS4 L389S mutant yields insights into senataxin post-translational modification and uncovers mutant-specific binding with a brain cytoplasmic RNA-encoded peptide. PLoS One. 2013;8:e78837. - PMC - PubMed
    1. Bentley D. The mRNA assembly line: transcription and processing machines in the same factory. Curr Opin Cell Biol. 2002;14:336–342. - PubMed

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