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Exploring the multifunctionality of SR proteins
Author(s) -
Irena Slišković,
Hannah Eich,
Michaela Müller-McNicoll
Publication year - 2021
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20210325
Subject(s) - sr protein , rna splicing , rna binding protein , alternative splicing , splicing factor , cytoplasm , computational biology , biology , rna processing , rna , heterogeneous ribonucleoprotein particle , transcription (linguistics) , microbiology and biotechnology , genetics , gene , messenger rna , linguistics , philosophy
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.

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