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.
Chen
Jing-Sen
JS
Neurosurgery Department, Second Affiliated Hospital of Zhejiang University, Hangzhou, 310009, China.
Hu
Hai-Ying
HY
Zhang
Shuo
S
He
Min
M
Hu
Ren-Ming
RM
D002460:Cell Line; D006801:Humans; D047468:Immunoprecipitation; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D025941:Protein Interaction Mapping; D017027:Protein Tyrosine Phosphatases; D008941:Spindle Apparatus / Q000737:chemistry; D020798:Two-Hybrid System Techniques; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
D025801:Ubiquitin; C111164:BRAP protein, human; D044767:Ubiquitin-Protein Ligases; D010744:Phosphoric Monoester Hydrolases; C120902:CDC14A protein, human; D017027:Protein Tyrosine Phosphatases