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A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.

Citation

Claudia Carissimi, Jennifer Baccon, Marco Straccia, Pieranna Chiarella, Alessio Maiolica, Alan Sawyer, Juri Rappsilber, Livio Pellizzoni. Unrip is a component of SMN complexes active in snRNP assembly. FEBS letters. 2005 Apr 25;579(11):2348-54

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PMID: 15848170

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