Unrip is a component of SMN complexes active in snRNP assembly

Claudia Carissimi, Jennifer Baccon, Marco Straccia, Pieranna Chiarella, Alessio Maiolica, Alan Sawyer, Juri Rappsilber, Livio Pellizzoni

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63 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2348-2354
Number of pages7
JournalFEBS Letters
Volume579
Issue number11
DOIs
StatePublished - Apr 25 2005

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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