LSm1 homolog, mRNA degradation associated protein (LSm1)

LSm1 homolog is a member of the Sm-like (LSm) family of proteins, forming part of a heptameric ring complex (LSm1-7) that is highly conserved from yeast to humans[2][4]. The primary role of the LSm1-7 complex is to participate in cytoplasmic mRNA degradation by promoting decapping and 5′–3′ exonucleolytic decay. LSm1-7, often in conjunction with the protein Pat1, binds to the 3′ end of deadenylated mRNA molecules, facilitating decapping by the Dcp1/Dcp2 enzyme complex and enabling degradation by exonucleases such as Xrn1[1][3][4]. LSm1 is thus a key regulator of mRNA turnover, controls histone mRNA decay, and contributes to the dynamics of RNA processing bodies (P-bodies) in the cytoplasm[2][5][6]. Misregulation or overexpression of LSm1 has been observed in cancer, and it plays a role in maintaining genomic stability and posttranscriptional gene control[6]. However, LSm1 itself is not currently a direct therapeutic target and there are no known interacting drugs or clinical biomarkers directly associated with this protein.

Other names

U6 snRNA-associated Sm-like protein LSm1CASMYJL124CCancer-associated Sm-like proteinSmall nuclear ribonucleoprotein CaSmcancer-associated Sm proteinFICUSLSM1 homologU6 small nuclear RNA-associated proteinLSM1 mRNA degradation associatedLSM1-like protein U6 small nuclear RNA-associated