2012
DOI: 10.1002/iub.1075
|View full text |Cite
|
Sign up to set email alerts
|

Regulating the regulators: Serine/arginine‐rich proteins under scrutiny

Abstract: SummarySerine/arginine-rich (SR) proteins are among the most studied splicing regulators. They constitute a family of evolutionarily conserved proteins that, apart from their initially identified and deeply studied role in splicing regulation, have been implicated in genome stability, chromatin binding, transcription elongation, mRNA stability, mRNA export and mRNA translation. Remarkably, this list of SR protein activities seems far from complete, as unexpected functions keep being unraveled. An intriguing as… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

1
30
0

Year Published

2013
2013
2022
2022

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 30 publications
(31 citation statements)
references
References 64 publications
1
30
0
Order By: Relevance
“…Last but not least, posttranslational modifications may also play a key role in ABA regulation of plant SR proteins. Indeed, aside from the well-established phosphorylation of RS domains to regulate protein-protein interactions and subcellular localization of SR proteins [100], several other modifications such as lysine acetylation, arginine methylation, ubiquitination or SUMO conjugation have been reported in animal systems to regulate SR protein degradation, stability and localization [101]. The regulation of SR gene expression is thus a decidedly complex affair involving multiple levels of control, and the mechanisms underlying ABA-regulated expression of plant SR/SR-like proteins, as well as their involvement in the ABA pathway, await further study.…”
Section: Discussionmentioning
confidence: 99%
“…Last but not least, posttranslational modifications may also play a key role in ABA regulation of plant SR proteins. Indeed, aside from the well-established phosphorylation of RS domains to regulate protein-protein interactions and subcellular localization of SR proteins [100], several other modifications such as lysine acetylation, arginine methylation, ubiquitination or SUMO conjugation have been reported in animal systems to regulate SR protein degradation, stability and localization [101]. The regulation of SR gene expression is thus a decidedly complex affair involving multiple levels of control, and the mechanisms underlying ABA-regulated expression of plant SR/SR-like proteins, as well as their involvement in the ABA pathway, await further study.…”
Section: Discussionmentioning
confidence: 99%
“…In plants, SR proteins have been investigated for their function in splicing (Lopato et al, 1999a(Lopato et al, , 1999b. In animal systems, SR proteins, apart from their role in pre-mRNA splicing, function in diverse processes associated with RNA metabolism and gene regulation, including mRNA export, stability and translation, chromatin binding, transcription elongation, subcellular localization of transcripts, genome stability and formation of cellular RNA granules, and miRNA processing structures (stress granules and processing bodies) (Long and Caceres, 2009;Shepard and Hertel, 2009;Risso et al, 2012;Yoon et al, 2013). Whether plant SR proteins, like their animal counterparts, have wide-ranging roles in other aspects of RNA metabolism remains to be seen.…”
Section: Trans-acting Factorsmentioning
confidence: 99%
“…Recent studies support the role of SR proteins not only as splicing regulators, but also implicate these proteins in genome stability, chromatin binding, transcription elongation, mRNA stability, mRNA export, and translation (see review 23 ). The function of SR proteins is regulated by phosphorylation and de-phosphorylation.…”
mentioning
confidence: 99%
“…Indeed, SR proteins undergo acetylation, methylation, and also ubiquitinylation (Ub), as well as modification by the small Ubiquitin-like modifier (SUMO). 23 Ub conjugation to SR proteins was suggested to serve as regulatory signal, rather than to direct the protein for degradation.…”
mentioning
confidence: 99%