U7 snRNA-associated Sm-like protein LSm11 (LSM11)

LSM11 is an Sm-like protein specifically incorporated into the U7 snRNP complex, replacing canonical Sm proteins in this specialized ribonucleoprotein particle[1]. It is distinguished by its unusually large size and the presence of extended N-terminal and intervening regions. The N-terminal region of LSM11 is essential for proper histone pre-mRNA 3'-end processing, binding both RNA and protein partners – notably interacting with ZFP100, which mediates recruitment and stabilization of histone RNA processing complexes[1]. Functionally, LSM11 is required for the accurate and efficient generation of non-polyadenylated replication-dependent histone mRNAs, and uniquely, the U7 snRNP complex represses histone gene transcription when the cell cycle is arrested (an activity modulated via interaction with hnRNP UL1)[2]. LSM11’s role is highly specialized to the molecular machinery that maintains strict control over histone synthesis within the cell cycle. No drugs or clinical biomarkers exist for LSM11, and it is not considered a therapeutic target in current research.

Other names

LSM11U7 snRNA-associated Sm-like protein LSm11FLJ38273AGS8

Not applicable (No drugs target this molecule.)