, Volume 114, Issue 3, pp 155–166 | Cite as

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

  • Hongzhi Xu
  • Ramesh S. Pillai
  • Teldja N. Azzouz
  • Karl B. Shpargel
  • Christian Kambach
  • Michael D. Hebert
  • Daniel Schümperli
  • A. Gregory Matera
Research Article


Coilin is the signature protein of the Cajal body (CB), a nuclear suborganelle involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs). Newly imported Sm-class snRNPs are thought to traffic through CBs before proceeding to their final nuclear destinations. Loss of coilin function in mice leads to significant viability and fertility problems. Coilin interacts directly with the spinal muscular atrophy (SMA) protein via dimethylarginine residues in its C-terminal domain. Although coilin hypomethylation results in delocalization of survival of motor neurons (SMN) from CBs, high concentrations of snRNPs remain within these structures. Thus, CBs appear to be involved in snRNP maturation, but factors that tether snRNPs to CBs have not been described. In this report, we demonstrate that the coilin C-terminal domain binds directly to various Sm and Lsm proteins via their Sm motifs. We show that the region of coilin responsible for this binding activity is separable from that which binds to SMN. Interestingly, U2, U4, U5, and U6 snRNPs interact with the coilin C-terminal domain in a glutathione S-transferase (GST)-pulldown assay, whereas U1 and U7 snRNPs do not. Thus, the ability to interact with free Sm (and Lsm) proteins as well as with intact snRNPs, indicates that coilin and CBs may facilitate the modification of newly formed snRNPs, the regeneration of ‘mature’ snRNPs, or the reclamation of unassembled snRNP components.


Spinal Muscular Atrophy Cajal Body Nuclear Speckle HeLa Nuclear Extract Spliceosomal snRNPs 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



We thank R. Lührmann, C.L. Will, and H. Salz for providing us with reagents used in this work. Moreover, we acknowledge financial support by the Novartis Foundation, the State of Bern, the Swiss National Science Foundation, the Muscular Dystrophy Association of the USA, and the US National Institutes of Health (R01 grants GM53034 and NS41617).


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Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • Hongzhi Xu
    • 1
  • Ramesh S. Pillai
    • 2
    • 5
  • Teldja N. Azzouz
    • 2
  • Karl B. Shpargel
    • 3
  • Christian Kambach
    • 4
  • Michael D. Hebert
    • 1
    • 3
  • Daniel Schümperli
    • 2
  • A. Gregory Matera
    • 3
  1. 1.Department of BiochemistryThe University of Mississippi Medical CenterJacksonUSA
  2. 2.Institute of Cell BiologyUniversity of BernBernSwitzerland
  3. 3.Department of GeneticsCase Western Reserve UniversityClevelandUSA
  4. 4.Paul Scherrer InstituteLife SciencesVilligen PSISwitzerland
  5. 5.Friedrich Miescher InstituteBaselSwitzerland

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