Correction: The deubiquitylase USP9X controls ribosomal stalling
نویسندگان
چکیده
منابع مشابه
USP45 deubiquitylase controls ERCC1–XPF endonuclease-mediated DNA damage responses
Reversible protein ubiquitylation plays important roles in various processes including DNA repair. Here, we identify the deubiquitylase USP45 as a critical DNA repair regulator. USP45 associates with ERCC1, a subunit of the DNA repair endonuclease XPF-ERCC1, via a short acidic motif outside of the USP45 catalytic domain. Wild-type USP45, but not a USP45 mutant defective in ERCC1 binding, effici...
متن کاملUSP9X Controls EGFR Fate by Deubiquitinating the Endocytic Adaptor Eps15
Following activation by its cognate ligand(s), the epidermal growth factor receptor (EGFR) is rapidly routed to the lysosome for degradation in a ubiquitination-dependent fashion. This pathway represents the major mechanism of long-term attenuation of EGFR signaling, and its deregulation is a significant feature in different types of cancers. Here we demonstrate, through a systematic RNAi-based...
متن کاملThe force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment for initial protein folding events. Here, we present a 2.9 Å cryo-electron microscopy structure of a ribosome stalled during translation of the e...
متن کاملFAM/USP9x, a Deubiquitinating Enzyme Essential for TGFβ Signaling, Controls Smad4 Monoubiquitination
The assembly of the Smad complex is critical for TGFbeta signaling, yet the mechanisms that inactivate or empower nuclear Smad complexes are less understood. By means of siRNA screen we identified FAM (USP9x), a deubiquitinase acting as essential and evolutionarily conserved component in TGFbeta and bone morphogenetic protein signaling. Smad4 is monoubiquitinated in lysine 519 in vivo, a modifi...
متن کاملUSP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1
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 initiatio...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2021
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.20200421102102021c