Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP

FEBS Letters

Rose, Stephen A.¹  Robinson, Philip A.¹  Markham, Alexander F.¹  Scott, Gina B.¹  Tan, Nancy G.S.¹  Ardley, Helen C.¹ 

[1] Molecular Medicine Unit, Level 6, Clinical Sciences Building, St James's University Hospital, Leeds LS9 7TF, UK

关键词: Human homologue of ariadne;    Translation initiation factor 4E homologous protein;    Ubiquitin-conjugating enzyme;    Ubiquitin-protein ligase;    Ubiquitin;    E2;    ubiquitin-conjugating enzyme;    E3;    ubiquitin-protein ligase;    4EHP;    translation initiation factor 4E homologous protein;    RING;    really interesting gene;    IBR;    in between RING;    HHARI;    human homologue of ariadne;    PBS;    phosphate-buffered saline;    eIF;    translation initiation factor;   

DOI  :  10.1016/S0014-5793(03)01235-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human homologue of Drosophila ariadne (HHARI) is a RING-IBR-RING domain protein identified through its ability to bind the human ubiquitin-conjugating enzyme, UbcH7. We now demonstrate that HHARI also interacts with the eukaryotic mRNA cap binding protein, translation initiation factor 4E homologous protein (4EHP), via the N-terminal RING1 finger of HHARI. HHARI, 4EHP and UbcH7 do not form a stable heterotrimeric complex as 4EHP cannot immunoprecipitate UbcH7 even in the presence of HHARI. Overexpression of 4EHP and HHARI in mammalian cells leads to polyubiquitylation of 4EHP. By contrast, HHARI does not promote its own autoubiquitylation. Thus, by promoting the ubiquitin-mediated degradation of 4EHP, HHARI may have a role in both protein degradation and protein translation.

【 授权许可】

Unknown