Downloaded from rnajournal.cshlp.org on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press SRSF10: an atypical splicing regulator with critical roles in stress response, organ development and viral replication Lulzim Shkreta1, Aurélie Delannoy1, Anna Salvetti2 and Benoit Chabot1* 1RNA group Department of Microbiology and Infectious Diseases Faculty of Medicine and Health Sciences Université de Sherbrooke Sherbrooke, Quebec, Canada 2INSERM, U1111, Centre International de Recherche en Infectiologie de Lyon (CIRI) CNRS UMR 5308 Lyon, France To whom correspondence should be addressed:
[email protected] Tel: (819) 821‐8000 ext 75321 Fax: (819) 820‐6831 Shkreta et al. 1 Downloaded from rnajournal.cshlp.org on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press Abstract Serine/Arginine Splicing Factor 10 (SRSF10) is a member of the family of mammalian splicing regulators known as SR proteins. Like several of its SR siblings, the SRSF10 protein is composed of an RNA binding domain (RRM) and of arginine and serine‐rich auxiliary domains (RS) that guide interactions with other proteins. The phosphorylation status of SRSF10 is of paramount importance for its activity and is subjected to changes during mitosis, heat‐shock and DNA damage. SRSF10 overexpression has functional consequences in a growing list of cancers. By controlling the alternative splicing of specific transcripts, SRSF10 has also been implicated in glucose, fat and cholesterol metabolism, in the development of the embryonic heart and in neurological processes. SRSF10 is also important for the proper expression and processing of HIV‐1 and other viral transcripts. We discuss how SRSF10 could become a potentially appealing therapeutic target to combat cancer and viral infections.