This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Massenet, S.
Right arrow Articles by Dreyfuss, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Massenet, S.
Right arrow Articles by Dreyfuss, G.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, September 2002, p. 6533-6541, Vol. 22, No. 18
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.18.6533-6541.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The SMN Complex Is Associated with snRNPs throughout Their Cytoplasmic Assembly Pathway

Séverine Massenet,1 Livio Pellizzoni,1 Sergey Paushkin,1 Iain W. Mattaj,2 and Gideon Dreyfuss1*

Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148,1 European Molecular Biology Laboratory, D-69117 Heidelberg, Germany2

Received 20 March 2002/ Returned for modification 2 May 2002/ Accepted 14 June 2002

The common neurodegenerative disease spinal muscular atrophy is caused by reduced levels of the survival of motor neurons (SMN) protein. SMN associates with several proteins (Gemin2 to Gemin6) to form a large complex which is found both in the cytoplasm and in the nucleus. The SMN complex functions in the assembly and metabolism of several RNPs, including spliceosomal snRNPs. The snRNP core assembly takes place in the cytoplasm from Sm proteins and newly exported snRNAs. Here, we identify three distinct cytoplasmic SMN complexes, each representing a defined intermediate in the snRNP biogenesis pathway. We show that the SMN complex associates with newly exported snRNAs containing the nonphosphorylated form of the snRNA export factor PHAX. The second SMN complex identified contains assembled Sm cores and m3G-capped snRNAs. Finally, the SMN complex is associated with a preimport complex containing m3G-capped snRNP cores bound to the snRNP nuclear import mediator snurportin1. Thus, the SMN complex is associated with snRNPs during the entire process of their biogenesis in the cytoplasm and may have multiple functions throughout this process.

* Corresponding author. Mailing address: Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148. Phone: (215) 898-0398. Fax: (215) 573-2000. E-mail: gdreyfuss{at}hhmi.upenn.edu.

Molecular and Cellular Biology, September 2002, p. 6533-6541, Vol. 22, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.18.6533-6541.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Monecke, T., Dickmanns, A., Ficner, R. (2009). Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1. Nucleic Acids Res 37: 3865-3877 [Abstract] [Full Text]  
  • Hearst, S. M., Gilder, A. S., Negi, S. S., Davis, M. D., George, E. M., Whittom, A. A., Toyota, C. G., Husedzinovic, A., Gruss, O. J., Hebert, M. D. (2009). Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines. J. Cell Sci. 122: 1872-1881 [Abstract] [Full Text]  
  • Patel, S. B., Bellini, M. (2008). The assembly of a spliceosomal small nuclear ribonucleoprotein particle. Nucleic Acids Res 36: 6482-6493 [Abstract] [Full Text]  
  • Scofield, D. G., Lynch, M. (2008). Evolutionary Diversification of the Sm Family of RNA-Associated Proteins. Mol Biol Evol 25: 2255-2267 [Abstract] [Full Text]  
  • Gonsalvez, G. B., Praveen, K., Hicks, A. J., Tian, L., Matera, A. G. (2008). Sm protein methylation is dispensable for snRNP assembly in Drosophila melanogaster. RNA 14: 878-887 [Abstract] [Full Text]  
  • Piazzon, N., Rage, F., Schlotter, F., Moine, H., Branlant, C., Massenet, S. (2008). In Vitro and in Cellulo Evidences for Association of the Survival of Motor Neuron Complex with the Fragile X Mental Retardation Protein. J. Biol. Chem. 283: 5598-5610 [Abstract] [Full Text]  
  • Watkins, N. J., Lemm, I., Luhrmann, R. (2007). Involvement of Nuclear Import and Export Factors in U8 Box C/D snoRNP Biogenesis. Mol. Cell. Biol. 27: 7018-7027 [Abstract] [Full Text]  
  • Sleeman, J. (2007). A regulatory role for CRM1 in the multi-directional trafficking of splicing snRNPs in the mammalian nucleus. J. Cell Sci. 120: 1540-1550 [Abstract] [Full Text]  
  • Carissimi, C., Saieva, L., Gabanella, F., Pellizzoni, L. (2006). Gemin8 Is Required for the Architecture and Function of the Survival Motor Neuron Complex. J. Biol. Chem. 281: 37009-37016 [Abstract] [Full Text]  
  • Girard, C., Neel, H., Bertrand, E., Bordonne, R. (2006). Depletion of SMN by RNA interference in HeLa cells induces defects in Cajal body formation. Nucleic Acids Res 34: 2925-2932 [Abstract] [Full Text]  
  • Carissimi, C., Saieva, L., Baccon, J., Chiarella, P., Maiolica, A., Sawyer, A., Rappsilber, J., Pellizzoni, L. (2006). Gemin8 Is a Novel Component of the Survival Motor Neuron Complex and Functions in Small Nuclear Ribonucleoprotein Assembly. J. Biol. Chem. 281: 8126-8134 [Abstract] [Full Text]  
  • Renvoise, B., Khoobarry, K., Gendron, M.-C., Cibert, C., Viollet, L., Lefebvre, S. (2006). Distinct domains of the spinal muscular atrophy protein SMN are required for targeting to Cajal bodies in mammalian cells. J. Cell Sci. 119: 680-692 [Abstract] [Full Text]  
  • den Engelsman, J., Gerrits, D., de Jong, W. W., Robbins, J., Kato, K., Boelens, W. C. (2005). Nuclear Import of {alpha}B-crystallin Is Phosphorylation-dependent and Hampered by Hyperphosphorylation of the Myopathy-related Mutant R120G. J. Biol. Chem. 280: 37139-37148 [Abstract] [Full Text]  
  • Grimmler, M., Otter, S., Peter, C., Muller, F., Chari, A., Fischer, U. (2005). Unrip, a factor implicated in cap-independent translation, associates with the cytosolic SMN complex and influences its intracellular localization. Hum Mol Genet 14: 3099-3111 [Abstract] [Full Text]  
  • Cote, J., Richard, S. (2005). Tudor Domains Bind Symmetrical Dimethylated Arginines. J. Biol. Chem. 280: 28476-28483 [Abstract] [Full Text]  
  • Sleeman, J. E., Trinkle-Mulcahy, L., Prescott, A. R., Ogg, S. C., Lamond, A. I. (2003). Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivo. J. Cell Sci. 116: 2039-2050 [Abstract] [Full Text]  
  • Zeiner, G. M., Sturm, N. R., Campbell, D. A. (2003). Exportin 1 Mediates Nuclear Export of the Kinetoplastid Spliced Leader RNA. Eukaryot Cell 2: 222-230 [Abstract] [Full Text]  
  • Stanek, D., Rader, S. D., Klingauf, M., Neugebauer, K. M. (2003). Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies. JCB 160: 505-516 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»