title: Regulating the regulators: serine/arginine-rich proteins under scrutiny.
abstract: Serine/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 aspect that awaits further investigation is how the multiple tasks of SR proteins are concertedly regulated within mammalian cells. In this article, we first discuss recent findings regarding the regulation of SR protein expression, activity and accessibility. We dive into recent studies describing SR protein auto-regulatory feedback loops involving different molecular mechanisms such asunproductive splicing, microRNA-mediated regulation and translational repression. In addition, we take into account another step of regulation of SR proteins, presenting new findings about a variety of post-translational modifications by proteomics approaches and how some of these modifications can regulate SR protein sub-cellular localization or stability. Towards the end, we focus in two recently revealed functions of SR proteins beyond mRNA biogenesis and metabolism, the regulation of micro-RNA processing and the regulation of small ubiquitin-like modifier (SUMO) conjugation.
authors.affiliation: Instituto de Fisiología, Biología Molecular y Neurociencias - Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.
authors.forename: Guillermo
authors.initials: G
authors.lastname: Risso
authors.forename: Federico
authors.initials: F
authors.lastname: Pelisch
authors.forename: Ana
authors.initials: A
authors.lastname: Quaglino
authors.forename: Berta
authors.initials: B
authors.lastname: Pozzi
authors.forename: Anabella
authors.initials: A
authors.lastname: Srebrow
mesh_terms: D017398:Alternative Splicing; D000818:Animals; D017124:Conserved Sequence; D025461:Feedback, Physiological; D005786:Gene Expression Regulation; D006801:Humans; D035683:MicroRNAs; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000068103:Serine-Arginine Splicing Factors; D015398:Signal Transduction; D025841:Small Ubiquitin-Related Modifier Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D035683:MicroRNAs; D009687:Nuclear Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D000068103:Serine-Arginine Splicing Factors