Shuttling SR proteins: more than splicing factors
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Updated: May 30, 2026

A Reporter Based Cellular Assay for Monitoring Splicing Efficiency
Published on: September 15, 2021
Laure Twyffels1, Cyril Gueydan, Véronique Kruys
1Laboratoire de Biologie Moléculaire du Gène, Faculté des Sciences, Université Libre de Bruxelles, Gosselies, Belgium.
Abstract:
Serine-arginine (SR) proteins commonly designate a family of eukaryotic RNA binding proteins containing a protein domain composed of several repeats of the arginine-serine dipeptide, termed the arginine-serine (RS) domain. This protein family is involved in essential nuclear processes such as constitutive and alternative splicing of mRNA precursors. Besides participating in crucial activities in the nuclear compartment, several SR proteins are able to shuttle between the nucleus and the cytoplasm and to exert regulatory functions in the latter compartment. This review aims at discussing the properties of shuttling SR proteins with particular emphasis on their nucleo-cytoplasmic traffic and their cytoplasmic functions. Indeed, recent findings have unravelled the complex regulation of SR protein nucleo-cytoplasmic distribution and the diversity of cytoplasmic mechanisms in which these proteins are involved.
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