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Interaction between mnk2 and CBC^(VHL) ubiquitin ligase E3 complex

Science China(Life Sciences) 2006年第3期49卷 265-273页

作者： WANG Pingzhang, WANG Xin, WANG Feng, CAI Tianjing & LUO Ying Chinese National Human Genome Center, Beijing 100176, China Institute of Basic Medical Sciences, Chinese Acadamy of Medical Sciences, Beijing 100005, China Shanghai Genomics Inc., Shanghai 201203, China Chinese National Human Genome Center Beijing 100176 China Institute of Basic Medical Sciences Chinese Acadamy of Medical Sciences Beijing 100005 China Chinese National Human Genome Center Beijing 100176 China Shanghai Genomics Inc. Shanghai 201203 China

MAP kinase-interacting kinase-2 (mnk2) is one of the downstream kinases activated by MAP kinases. It phosphorylates the eukaryotic initiation factor 4E (eIF4E), although the role of eIF4E phosphorylation and the role of mnk2 in the process of protein translation are not well understood. Except for eIF4E, other physiological substrates of mnk2 are still unidentified. To look for these unidentified substrates and to reveal the physiological function of mnk2, we performed a yeast two-hybrid screening with mnk2 as the bait. The results demonstrated mnk2 could interact with VHL (von Hippel-Lindau tumor suppressor), Rbx1 (ring-box 1) and Cul2 (Cullin2) proteins in yeast cells. Furthermore, we validated the interaction between mnk2 and VHL proteins in mammalian cells by co-immunoprecipitation analysis. Because the three proteins VHL, Rbx1 and Cul2 are all components of the CBCVHL ubiquitin ligase E3 complex, it has been shown that mnk2 can interact with CBCVHL complex, and is probably one of the new substrates of the CBCVHL complex. Furthermore, during the interaction of mnk2 with von Hippel-Lindau (VHL) tumor suppressor- binding protein 1 (VBP1), it appears that mnk2 also joins to modulate cell shape as VBP1 plays an important role in the process of the maturation of the cytoskeleton and in the process of morphogenesis.

关键词： mnk2, yeast two-hybrid, CBCVHL ubiquitin ligase E3 complex, VBP1.

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