The eukaryotic Sm and Sm-like (Lsm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β-sheet [, , ]. Lsm11 is an SmD2-like subunit which binds U7 snRNA along with Lsm10 and five other Sm subunits to form a 7-membered ring structure. Lsm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing [, ].
This entry represents the middle domain of Lsm11.The eukaryotic Sm and Sm-like (Lsm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β-sheet [, , ]. Lsm11 is an SmD2-like subunit which binds U7 snRNA along with Lsm10 and five other Sm subunits to form a 7-membered ring structure. Lsm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing [, ].
CASP8-associated protein 2 (CASP8AP2), also known as FLASH, is involved in various cellular functions, such as cell cycle progression, transcriptional regulation, the regulation of apoptosis, and the regulation of histone gene expression []. It is an essential component of Cajal bodies and is involved in the apoptosis receptor signaling pathway [].FLASH contains the N terminus required for histone pre-mRNA processing, the C-terminal segment which forms a SANT/Myb-like domain, and a small central region which binds Ars2 essential for cell cycle progression []. Its N-terminal domain has been found to form a 2:1 heterotrimer with Lsm11 for histone pre-mRNA 3'-end processing [].
