Coumarin 153 (CAS 53518-18-6)

Sm-like proteins, often denoted as Lsm proteins, are a family of RNA-binding proteins that are structurally and functionally related to the Sm protein family. These proteins are generally found in eukaryotic cells and form hetero-oligomeric complexes, usually consisting of seven distinct but closely related Lsm subunits. These complexes are involved in various aspects of RNA metabolism, including mRNA decay, RNA splicing, and gene regulation. Specifically, the Lsm1-7 complex is known to be involved in mRNA decapping and subsequent degradation, whereas the Lsm2-8 complex is associated with the processing of spliceosomal U6 small nuclear RNA. Overall, the Sm-like protein complexes serve as critical components in RNA processing pathways, helping to regulate the stability, processing, and function of various RNA molecules within the cell. Like-Sm (LSm) Inhibitors would belong to a unique category of molecules designed to modulate the function or stability of LSm complexes or Sm-like proteins. LSm complexes are vital players in RNA metabolism and are involved in diverse cellular processes, such as mRNA degradation and splicing. These inhibitors could act through multiple modes of action. For instance, they might directly bind to the LSm proteins, disrupting their assembly into functional complexes. Alternatively, they could block the protein-RNA or protein-protein interactions crucial for LSm function. Yet another mode of action could involve the disruption of upstream pathways that regulate the expression or activation of LSm complexes, thus exerting an indirect effect.