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

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-1-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 alpha-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.

Pubmed ID: 11146551

Authors

  • Germani A
  • Bruzzoni-Giovanelli H
  • Fellous A
  • Gisselbrecht S
  • Varin-Blank N
  • Calvo F

Journal

Oncogene

Publication Data

December 7, 2000

Associated Grants

None

Mesh Terms

  • Cell Cycle
  • Cysteine Endopeptidases
  • DNA-Binding Proteins
  • Fluorescent Antibody Technique
  • Gene Expression Regulation
  • Humans
  • Kinesin
  • Mitosis
  • Multienzyme Complexes
  • Nuclear Proteins
  • Precipitin Tests
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Sequence Deletion
  • Substrate Specificity
  • Transfection
  • Tubulin
  • Tumor Cells, Cultured
  • Two-Hybrid System Techniques
  • Ubiquitin-Protein Ligases
  • Ubiquitins