ArticleScientific reports2017
Interaction profiling of RNA-binding ubiquitin ligases reveals a link between posttranscriptional regulation and the ubiquitin system.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
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- The nexus between RNA-binding proteins and their effectors.Nature reviews. Genetics · 2023Review
- The OTUD6B-LIN28B-MYC axis determines the proliferative state in multiple myeloma.The EMBO journal · 2022Article
- Transcriptome-Wide Identification of Coding and Noncoding RNA-Binding Proteins Defines the Comprehensive RNA Interactome of Leishmania mexicana.Microbiology spectrum · 2022Article
- RNA-Binding RING E3-Ligase DZIP3/hRUL138 Stabilizes Cyclin D1 to Drive Cell-Cycle and Cancer Progression.Cancer research · 2021Article
- New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response.Frontiers in molecular biosciences · 2021Review
- Plasticity of nuclear and cytoplasmic stress responses of RNA-binding proteins.Nucleic acids research · 2020Article
- Makorin 1 controls embryonic patterning by alleviating Bruno1-mediated repression of oskar translation.PLoS genetics · 2020Article
- The RNA-binding ubiquitin ligase MKRN1 functions in ribosome-associated quality control of poly(A) translation.Genome biology · 2019Article
- What Are 3' UTRs Doing?Cold Spring Harbor perspectives in biology · 2019Review
- Proteins that physically interact with the phosphatase Cdc14 in Candida albicans have diverse roles in the cell cycle.Scientific reports · 2019Article
- The DNA binding high mobility group box protein family functionally binds RNA.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA-binding ubiquitin ligases (RBULs) have the potential to link RNA-mediated mechanisms to protein ubiquitylation. Despite this, the cellular functions, substrates and interaction partners of most RBULs remain poorly characterized. Affinity purification (AP) combined with quantitative mass spectrometry (MS)-based proteomics is a powerful approach for analyzing protein functions. Mapping the physiological interaction partners of RNA-binding proteins has been hampered by their intrinsic properties, in particular the existence of low-complexity regions, which are prone to engage in non-physiological interactions. Here, we used an adapted AP approach to identify the interaction partners of human RBULs harboring different RNA-binding domains. To increase the likelihood of recovering physiological interactions, we combined control and bait-expressing cells prior to lysis. In this setup, only stable interactions that were originally present in the cell will be identified. We exploit gene function similarity between the bait proteins and their interactors to benchmark our approach in its ability to recover physiological interactions. We reveal that RBULs engage in stable interactions with RNA-binding proteins involved in different steps of RNA metabolism as well as with components of the ubiquitin conjugation machinery and ubiquitin-binding proteins. Our results thus demonstrate their capacity to link posttranscriptional regulation with the ubiquitin system.
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