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      pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.

      Molecular and Cellular Biology

      Blotting, Western, Cell Nucleus, metabolism, Chloride Channels, physiology, Cytosol, Immunochemistry, Ion Channels, Models, Biological, Oocytes, Protein Binding, Recombinant Fusion Proteins, Ribonucleoproteins, Small Nuclear, biosynthesis, Spliceosomes, Xenopus Proteins, Xenopus laevis, Animals

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          Abstract

          The U1, U2, U4, U5, and U6 small nuclear ribonucleoproteins (snRNPs) form essential components of spliceosomes, the machinery that removes introns from pre-mRNAs in eukaryotic cells. A critical initial step in the complex process of snRNP biogenesis is the assembly of a group of common core proteins (Sm proteins) on spliceosomal snRNA. In this study we show by multiple independent methods that the protein pICln associates with Sm proteins in vivo and in vitro. The binding of pICln to Sm proteins interferes with Sm protein assembly on spliceosomal snRNAs and inhibits import of snRNAs into the nucleus. Furthermore, pICln prevents the interaction of Sm proteins with the survival of motor neurons (SMN) protein, an interaction that has been shown to be critical for snRNP biogenesis. These findings lead us to propose a model in which pICln participates in the regulation of snRNP biogenesis, at least in part by interfering with Sm protein interaction with SMN protein.

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          Journal
          10330151
          104370

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