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.
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
Oncogene
Date: Dec. 07, 2000
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