Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways.

@article{Ralser2005Ataxin2AH,
  title={Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways.},
  author={Markus Ralser and Ute Nonhoff and Mario Albrecht and Thomas Lengauer and Erich E. Wanker and Hans Lehrach and Sylvia Krobitsch},
  journal={Human molecular genetics},
  year={2005},
  volume={14 19},
  pages={2893-909}
}
Spinocerebellar ataxia type 2 is an inherited neurodegenerative disorder that is caused by an expanded trinucleotide repeat in the SCA2 gene, encoding a polyglutamine stretch in the gene product ataxin-2. Although evidence has been provided that ataxin-2 is involved in RNA metabolism, the physiological function of ataxin-2 remains unclear. Here, we demonstrate that ataxin-2 interacts with two members of the endophilin family, endophilin-A1 and endophilin-A3. To elucidate the physiological… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 47 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 95 references

Differential expression of endophilin 1 and 2 dimers at central nervous system synapses

  • N. Ringstad, Y. Nemoto, P. De Camilli
  • J. Biol. Chem.,
  • 2001
Highly Influential
3 Excerpts

Molecular basis for dissimilar nuclear trafficking of the actin - bundling protein isoforms T - and L - plastin

  • A. Giganti, J. Plastino, +5 authors E. Friederich
  • 2005

Molecular basis for dissimilar nuclear trafficking of the actin-bundling protein isoforms

  • V. Delanote, K. Van Impe, +7 authors J. Gettemans
  • T- and L-plastin. Traffic,
  • 2005
1 Excerpt

Similar Papers

Loading similar papers…