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Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP
Author(s) -
Tan Nancy G.S.,
Ardley Helen C.,
Scott Gina B.,
Rose Stephen A.,
Markham Alexander F.,
Robinson Philip A.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01235-3
Subject(s) - ubiquitin , microbiology and biotechnology , heterotrimeric g protein , ubiquitin conjugating enzyme , initiation factor , ring finger , biology , eukaryotic translation , ubiquitin ligase , translation (biology) , biochemistry , messenger rna , signal transduction , gene , g protein
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.