Can Changes in SR Protein Acetylation Affect Alternative Splicing?

Cellular phenotype and function is determined by the cellular proteome. Within the cellular proteome there are processes that have a potential to significantly alter the composition of the proteome. One such process is called alternative splicing. Splicing is the removal of introns from a pre-mRNA sequence and the remaining pre-mRNA sequences, called exons, are combined. Alternative splicing modifies the intron-exon combination, and can form novel products from the different arrangement of the coding sequences. The misreguation of alternative splicing has been documented in many human diseases. The regulation of alternative splicing involves a complex network of proteins and RNA. Serine-arginine repeat (SR) proteins are a known family of regulatory proteins that bind within exons to promote exon inclusion into the mature mRNA transcript. SR protein activity is regulated by the post-translational modifications, phosphorylation and acetylation. The enclosed study proposes a possible mechanism of how the acetylation of SR proteins can alter alternative splicing. This book should be helpful to anyone interested in the regulation of alternative splicing and SR proteins.