Role of Survival Motor Neuron Complex Components in Small Nuclear Ribonucleoprotein Assembly*

@article{Ogawa2009RoleOS,
  title={Role of Survival Motor Neuron Complex Components in Small Nuclear Ribonucleoprotein Assembly*},
  author={Chihiro Ogawa and Kengo Usui and Fuyu Ito and Masayoshi Itoh and Yoshihide Hayashizaki and Harukazu Suzuki},
  journal={Journal of Biological Chemistry},
  year={2009},
  volume={284},
  pages={14609 - 14617}
}
Survival motor neuron (SMN) complex is essential for the biogenesis of the small nuclear ribonucleoprotein (snRNP) complex, although the complete role of each SMN complex component for the snRNP synthesis is largely unclear. We have identified an interaction between the two components Gemin2-Gemin7 using the mammalian two-hybrid system. In vitro stability assay revealed that the known SMN-Gemin7 interaction becomes stable in the presence of Gemin2 possibly via the identified Gemin2-Gemin7… 

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References

SHOWING 1-10 OF 49 REFERENCES

Gemin8 Is Required for the Architecture and Function of the Survival Motor Neuron Complex*

The essential role of Gemin8 is revealed for the proper structural organization of the SMN complex and the involvement of the heteromeric subunit containing Gemin6, Gemin7,Gemin8, and Unrip in the recruitment of Sm proteins to the snRNP assembly pathway is revealed.

Gemin8 Is a Novel Component of the Survival Motor Neuron Complex and Functions in Small Nuclear Ribonucleoprotein Assembly*

It is demonstrated that Gemin8 is a novel integral component of the SMN complex and extend the repertoire of cellular proteins involved in the pathway of snRNP biogenesis.

Gemin2 Plays an Important Role in Stabilizing the Survival of Motor Neuron Complex*

Results indicate that Gemin2 plays an important role in snRNP assembly through the stabilization of the SMN oligomer/complex via novel self-interaction through a novel interaction with amino-terminal SMN missense mutants.

Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins.

  • K. ShpargelA. Matera
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2005
The results identify a previously uncharacterized function for Gemin3 and Gemin4 in Sm core assembly and correlate the activity of this pathway with SMA, and demonstrate that Cajal body homeostasis requires SMN and ongoing snRNP biogenesis.

Unrip, a factor implicated in cap-independent translation, associates with the cytosolic SMN complex and influences its intracellular localization.

Interestingly, RNAi-induced reduction of unrip protein levels leads to enhanced accumulation of SMN in the nucleus as evident by the increased formation of nuclear gems/Cajal bodies, and it is speculated that unrip plays a crucial role in the intracellular distribution of the SMN complex.

Identification and Characterization of Gemin7, a Novel Component of the Survival of Motor Neuron Complex*

A novel protein component of the SMN complex termed Gemin7 is identified using native purified SMN complexes and peptide sequencing by mass spectrometry and interacts with several Sm proteins of spliceosomal small nuclear ribonucleoproteins, in particular, with SmE.

A Comprehensive Interaction Map of the Human Survival of Motor Neuron (SMN) Complex*

A comprehensive interaction map of all core components of the SMN complex is presented based upon in vivo and in vitro methods and it is shown that the peripheral component Gemin5 contributes an essential activity to theSMN complex, most likely the transfer of Sm proteins onto the U snRNA.

Sequence‐specific interaction of U1 snRNA with the SMN complex

It is shown that SMN complex interaction with SL1 is sequence‐specific and critical for U1 snRNP biogenesis, further supporting the direct role of the SMNcomplex in RNP biogenic.