Abstract
Members of the arginine–serine-rich protein family (SR proteins) are multifunctional RNA-binding proteins that have emerged as key determinants for mRNP formation, identity and fate. They bind to pre-mRNAs early during transcription in the nucleus and accompany bound transcripts until they are translated or degraded in the cytoplasm. SR proteins are mostly known for their essential roles in constitutive splicing and as regulators of alternative splicing. However, many additional activities of individual SR proteins, beyond splicing, have been reported in recent years. We will summarize the different functions of SR proteins and discuss how multifunctionality can be achieved. We will also highlight the difficulties of studying highly versatile SR proteins and propose approaches to disentangle their activities, which is transferrable to other multifunctional RBPs.
Highlights
Serine/arginine-rich splicing factors (SRSFs, SR proteins) are a phylogenetically conserved family of RNA-binding proteins (RBPs) present in all metazoans and plants [1]
Described as essential regulators of constitutive and alternative pre-mRNA splicing [2,3], we know that SR proteins influence all steps in the life cycle of mRNAs from transcription, splicing, polyadenylation and mRNP packing in the nucleus to mRNA export, translation and decay in the cytoplasm [3,4,5]
Apart from canonical and non-canonical functions in mRNA metabolism, SR proteins participate in the processing of non-coding RNAs, the regulation of post-translational modifications (PTMs), and the formation and dynamics of nuclear compartments [6,7,8,9]
Summary
Serine/arginine-rich splicing factors (SRSFs, SR proteins) are a phylogenetically conserved family of RNA-binding proteins (RBPs) present in all metazoans and plants [1]. Phosphorylated RS domains are required for the recruitment of SR proteins to transcription sites and spliceosome assembly, while RS dephosphorylation promotes splicing catalysis, mRNP packaging and nuclear export [18,36].
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