SIAH-1 interacts with α-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis

Antonia Germani, Heriberto Bruzzoni-Giovanelli, Arlette Fellous, Sylvie Gisselbrecht, Nadine Varin-Blank, Fabien Calvo

Research output: Contribution to journalArticle

Abstract

SIAH-1, a human homologue of the Drosophila seven in absentia (Sina), has been implicated in ubiquitin-mediated proteolysis of different target proteins through its N-terminal RING finger domain. SIAH-1 is also induced during p53-mediated apoptosis. Furthermore, SIAH-l-transfected breast cancer cell line MCF-7 exhibits an altered mitotic process resulting in multinucleated giant cells. Now, using the two-hybrid system, we identified two new SIAH interacting proteins: Kid (kinesin like DNA binding protein) and α-tubulin. We demonstrate that SIAH is involved in the degradation of Kid via the ubiquitin-proteasome pathway. Our results suggest that SIAH-1 but not its N-terminal deletion mutant, affects the mitosis by an enhanced reduction of kinesin levels. Our results imply, for the first time, SIAH-1 in regulating the degradation of proteins directly implicated in the mitotic process.

Original languageEnglish
Pages (from-to)5997-6006
Number of pages10
JournalOncogene
Volume19
Issue number52
DOIs
Publication statusPublished - Dec 7 2000

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Keywords

  • Kid
  • Kinesin
  • Mitosis
  • SIAH-1
  • Ubiquitin degradation

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

Cite this

Germani, A., Bruzzoni-Giovanelli, H., Fellous, A., Gisselbrecht, S., Varin-Blank, N., & Calvo, F. (2000). SIAH-1 interacts with α-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. Oncogene, 19(52), 5997-6006. https://doi.org/10.1038/sj.onc.1204002