SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates.

@article{Sittler1998SH3GL3AW,
  title={SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates.},
  author={Annie Sittler and Stephanie Waelter and Niels Wedemeyer and Renate Hasenbank and Eberhard Scherzinger and Holger Eickhoff and Gillian P Bates and Hans Lehrach and Erich E. Wanker},
  journal={Molecular cell},
  year={1998},
  volume={2 4},
  pages={427-36}
}
The mechanism by which aggregated polygins cause the selective neurodegeneration in Huntington's disease (HD) is unknown. Here, we show that the SH3GL3 protein, which is preferentially expressed in brain and testis, selectively interacts with the HD exon 1 protein (HDex1p) containing a glutamine repeat in the pathological range and promotes the formation of insoluble polyglutamine-containing aggregates in vivo. The C-terminal SH3 domain in SH3GL3 and the proline-rich region in HDex1p are… CONTINUE READING
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