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LSM7 is a highly conserved Sm-like RNA-binding protein and a constituent of two essential multimeric complexes in eukaryotic cells. In the nucleus, LSM7 forms part of the LSM2–8 complex, which binds and stabilizes U6 small nuclear RNA to promote the fidelity and assembly of the spliceosome responsible for pre-mRNA splicing[1][4][8]. In the cytoplasm, LSM7 joins the LSM1–7–Pat1 complex, which binds oligoadenylated mRNAs to facilitate decapping and subsequent 5′–to–3′ mRNA degradation[2][4][6]. Disruption of LSM7's function adversely affects spliceosome assembly and mRNA decay, highlighting its centrality in maintaining cellular RNA homeostasis[4][6]. Experimental evidence also links LSM7 to breast cancer metastasis through indirect modulation of alternative splicing[7].
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