Brap2 facilitates HsCdc14A Lys-63 linked ubiquitin modification.

Protein phosphotase Cdc14 (Cell division cycle gene 14) is a key regulator of late mitotic events in Saccharomyces cerevisiae. However the function of human Cdc14 (HsCdc14A & B) and its regulatory network are still elusive. In this study, we identified a new partner of HsCdc14A named Brap2 (BRCA1 associated protein ...
2) using yeast two-hybrid screening assay. The interaction between these two proteins is confirmed by co-immunoprecipitation in human HEK 293T cells. Brap2 co-localizes with HsCdc14A on mitotic spindle poles and over-expression of Brap2 causes multiple spindle poles. Furthermore, we found that Brap2, which has intrinsic RING domain dependent E3 ligase activity, facilitates HsCdc14A Lys-63 linked ubiquitin modification, indicating that Brap2 may be the ubiquitin E3 Ligase of HsCdc14A. Our findings imply that Brap2 plays a significant role in cell cycle regulation besides its facilitation of HsCdc14A ubiquitination.
Mesh Terms:
Cell Line, Humans, Immunoprecipitation, Mitotic Spindle Apparatus, Phosphoric Monoester Hydrolases, Protein Interaction Mapping, Two-Hybrid System Techniques, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
Biotechnol. Lett.
Date: May. 01, 2009
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