USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1.

ABSTRACT: Controlling translation initiation is an efficient way to regulate gene expression at the post-transcriptional level. However, current knowledge regarding regulatory proteins and their modes of controlling translation initiation is still limited. In this study, we employed tandem affinity purification and mass spectrometry to screen for unknown proteins associated with the translation initiation machinery. Ubiquitin specific peptidase 9, X-linked (USP9X), was identified as a novel binding partner, that interacts with the eukaryotic translation initiation factor 4B (eIF4B) in a mRNA-independent manner. USP9X-deficient cells presented significantly impaired nascent protein synthesis, cap-dependent translation initiation and cellular proliferation. USP9X can selectively alter the translation

SUBMITTER: Li Z 

PROVIDER: S-EPMC5778534 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature