Structural investigations of the RNA-binding properties of STAR proteins

Abstract

STAR (signal transduction and activation of RNA) proteins are a family of RNA-binding proteins that regulate post-transcriptional gene regulation events at various levels, such as pre-mRNA alternative splicing, RNA export, translation and stability. Most of these proteins are regulated by signalling pathways through post-translational modifications, such as phosphorylation and arginine methylation. These proteins share a highly conserved RNA-binding domain, denoted STAR domain. Structural investigations of this STAR domain in complex with RNA have highlighted how a subset of STAR proteins specifically recognizes its RNA targets. The present review focuses on the structural basis of RNA recognition by this family of proteins.

Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly

“…Given that mammalian ERH forms homodimers in solution (Arai et al, 2005; Wan et al, 2005), it is possible that Erh1 mediates Mmi1 dimerization, thereby allowing Mmi1 to exert its RNA-binding activity in vivo . Indeed, dimerization is known to be a prerequisite for the function of STAR, which is a subfamily of KH domain-containing RNA-binding proteins (Feracci et al, 2014), and hnRNP C forms tetramers to measure RNA length (McCloskey et al, 2012). …”