The C-terminus of PARK2 is required for its self-interaction, solubility and role in the spindle assembly checkpoint
| Autor: | Yvan Chen, Yi-Cheng Chen, Shang-Ting Fang, Hsueh-Hui Yang, Chih-Jui Chang, Wei-Jun Zhai, Pei-Chi Yeh, Yue-Li Juang, Shin-Yuan Chen |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Cell cycle checkpoint
Ubiquitin-Protein Ligases Blotting Western Mitosis Spindle Apparatus Biology Spindle assembly checkpoint Spindle pole body chemistry.chemical_compound Humans Molecular Biology Centrosome Kinetochore Circular Dichroism Self-interaction G2-M DNA damage checkpoint PARK2 Cell biology Spindle apparatus Spindle checkpoint Nocodazole Microscopy Fluorescence Solubility chemistry Molecular Medicine Anaphase-promoting complex HeLa Cells |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. (4):573-580 |
| ISSN: | 0925-4439 |
| DOI: | 10.1016/j.bbadis.2011.12.007 |
| Popis: | PARK2, an ubiquitin ligase closely correlated with Parkinson's disease and cancer, has been shown to accumulate at centrosomes to ubiquitinate misfolded proteins accumulated during interphase. In the present study, we demonstrated that PARK2 can also localize to centrosomes in mitosis and that the protein does not fluctuate through the S- to M-phase. A C-terminal truncation of PARK2 resulted in a spindle assembly checkpoint defect, characterized by HeLa cells able to bypass mitotic arrest induced by nocodazole and form multinucleated cells when overexpressing the C-terminal truncated PARK2 protein. The spindle assembly checkpoint defect may be due to a change in a biochemical or structural property of PARK2 caused by the C-terminal truncation, resulting in a loss of self-interaction between PARK2 proteins. |
| Databáze: | OpenAIRE |
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