Unrip is a component of SMN complexes active in snRNP assembly

Citations of this article
Mendeley users who have this article in their library.


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. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.




Carissimi, C., Baccon, J., Straccia, M., Chiarella, P., Maiolica, A., Sawyer, A., … Pellizzoni, L. (2005). Unrip is a component of SMN complexes active in snRNP assembly. FEBS Letters, 579(11), 2348–2354. https://doi.org/10.1016/j.febslet.2005.03.034

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free