Roles of Sumoylation in mRNA Processing and Metabolism

Richard, Patricia; Vethantham, Vasupradha; Manley, James L.

doi:10.1007/978-3-319-50044-7_2

Cited by 28 publications

(26 citation statements)

References 152 publications

(228 reference statements)

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“…In addition, SUMOylation might play roles in the known functions of these proteins. While the role of SUMOylation in RNA splicing and mRNA transport has not been extensively studied, heterogeneous nuclear RNA binding proteins (hnRNPs), which have multiple roles in RNA splicing stabilization and export, are highly SUMOylated by both SUMO1 and SUMO2/3 [ 82 – 84 ]. In addition, the RanBP2/Nup358 component of the nuclear pore complex, which plays roles in mRNA export and translation, is a SUMO E3 ligase [ 36 , 85 , 86 ].…”

Section: Discussionmentioning

confidence: 99%

A genome-wide screen of Epstein-Barr virus proteins that modulate host SUMOylation identifies a SUMO E3 ligase conserved in herpesviruses

et al. 2018

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Many cellular processes pertinent for viral infection are regulated by the addition of small ubiquitin-like modifiers (SUMO) to key regulatory proteins, making SUMOylation an important mechanism by which viruses can commandeer cellular pathways. Epstein-Barr virus (EBV) is a master at manipulating of cellular processes, which enables life-long infection but can also lead to the induction of a variety of EBV-associated cancers. To identify new mechanisms by which EBV proteins alter cells, we screened a library of 51 EBV proteins for global effects on cellular SUMO1 and SUMO2 modifications (SUMOylation), identifying several proteins not previously known to manipulate this pathway. One EBV protein (BRLF1) globally induced the loss of SUMOylated proteins, in a proteasome-dependent manner, as well as the loss of promeylocytic leukemia nuclear bodies. However, unlike its homologue (Rta) in Kaposi’s sarcoma associated herpesvirus, it did not appear to have ubiquitin ligase activity. In addition we identified the EBV SM protein as globally upregulating SUMOylation and showed that this activity was conserved in its homologues in herpes simplex virus 1 (HSV1 UL54/ICP27) and cytomegalovirus (CMV UL69). All three viral homologues were shown to bind SUMO and Ubc9 and to have E3 SUMO ligase activity in a purified system. These are the first SUMO E3 ligases discovered for EBV, HSV1 and CMV. Interestingly the homologues had different specificities for SUMO1 and SUMO2, with SM and UL69 preferentially binding SUMO1 and inducing SUMO1 modifications, and UL54 preferentially binding SUMO2 and inducing SUMO2 modifications. The results provide new insights into the function of this family of conserved herpesvirus proteins, and the conservation of this SUMO E3 ligase activity across diverse herpesviruses suggests the importance of this activity for herpesvirus infections.

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Section: Discussionmentioning

confidence: 99%

A genome-wide screen of Epstein-Barr virus proteins that modulate host SUMOylation identifies a SUMO E3 ligase conserved in herpesviruses

et al. 2018

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“…CARM1 knock‐down enhances the nuclear retention of mRNAs containing inverted repeated Alu elements (IR Alu s), via reducing binding of NONO to target mRNAs . SUMOylation, ADP‐ribosylation and acetylation are also found in several proteomics studies, there should more in‐depth studies.…”

Section: Regulation Of Nono Expressionmentioning

confidence: 99%

NONO and tumorigenesis: More than splicing

Feng

Deng

et al. 2020

J Cellular Molecular Medi

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The NONO (non-POU domain-containing octamer-binding protein) protein, also known as 54 kD nuclear RNA-and DNA-binding protein (p54nrb), belongs to the multifunctional DBHS (Drosophila behaviour/human splicing) family of proteins which can bind DNA, RNA and protein. 1 NONO has a nuclear localization signal (NLS) at its C-terminal, so it is located in the nucleus of most mammalian cells and is primarily distributed in the subnuclear domain named paraspeckles. 2 Emerging evidence strongly indicates new roles for NONO in tumorigenesis, including but not limited to regulating proliferation, apoptosis, cell migration and DNA damage repair. Here, we provide a comprehensive review of the NONO and its functions in tumorigenesis. AbstractThe non-POU domain-containing octamer-binding protein NONO/p54 nrb , which belongs to the Drosophila behaviour/human splicing (DBHS) family, is a multifunctional nuclear protein rarely functioning alone. Emerging solid evidences showed that NONO engages in almost every step of gene regulation, including but not limited to mRNA splicing, DNA unwinding, transcriptional regulation, nuclear retention of defective RNA and DNA repair. NONO is involved in many biological processes including cell proliferation, apoptosis, migration and DNA damage repair. Dysregulation of NONO has been found in many types of cancer. In this review, we summarize the current and fast-growing knowledge about the regulation of NONO, its biological function and implications in tumorigenesis and cancer progression. Overall, significant findings about the roles of NONO have been made, which might make NONO to be a new biomarker or/and a possible therapeutic target for cancers. K E Y W O R D S DBHS, NONO, splicing, tumorigenesis | 4369 FENG Et al.

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“…According to a study, SUMO-1 and the E2-conjugating enzyme ubc9 are localized to Cajal bodies (sites of maturation of snRNPs) necessary for pre-mRNA processing ( Navascues et al, 2008 ). Multiple putative SUMO targets are present in functional capping, splicing, polyadenylation, termination, and mRNA export processes ( Richard et al, 2017 ). During heat stress, SUMOylation has been accounted for controlling DNA methylation patterns, which, along with the stress-up-regulated SUMOylation of Arabidopsis variants of histone acetylases/deacetylases, for example, GCN5/ADA2B ( Sterner et al, 2006 ) and HDA19 ( To et al, 2011 ), may then assist in the conversion of euchromatic regions into heterochromatic regions during stress.…”

Section: Chromatin Modifications In Plant Stress Tolerancementioning

confidence: 99%

Role of Chromatin Architecture in Plant Stress Responses: An Update

et al. 2021

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Sessile plants possess an assembly of signaling pathways that perceive and transmit environmental signals, ultimately resulting in transcriptional reprogramming. Histone is a key feature of chromatin structure. Numerous histone-modifying proteins act under different environmental stress conditions to help modulate gene expression. DNA methylation and histone modification are crucial for genome reprogramming for tissue-specific gene expression and global gene silencing. Different classes of chromatin remodelers including SWI/SNF, ISWI, INO80, and CHD are reported to act upon chromatin in different organisms, under diverse stresses, to convert chromatin from a transcriptionally inactive to a transcriptionally active state. The architecture of chromatin at a given promoter is crucial for determining the transcriptional readout. Further, the connection between somatic memory and chromatin modifications may suggest a mechanistic basis for a stress memory. Studies have suggested that there is a functional connection between changes in nuclear organization and stress conditions. In this review, we discuss the role of chromatin architecture in different stress responses and the current evidence on somatic, intergenerational, and transgenerational stress memory.

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Roles of Sumoylation in mRNA Processing and Metabolism

Cited by 28 publications

References 152 publications

A genome-wide screen of Epstein-Barr virus proteins that modulate host SUMOylation identifies a SUMO E3 ligase conserved in herpesviruses

A genome-wide screen of Epstein-Barr virus proteins that modulate host SUMOylation identifies a SUMO E3 ligase conserved in herpesviruses

NONO and tumorigenesis: More than splicing

Role of Chromatin Architecture in Plant Stress Responses: An Update

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