Identification of proximal SUMO-dependent interactors using SUMO-ID.
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent ... labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors of PML are involved in transcription, DNA damage, stress response and SUMO modification and are highly enriched in SUMO Interacting Motifs, but may only represent a subset of the total PML proximal proteome. Likewise, SUMO-ID also allow us to identify interactors of SUMOylated SALL1, a less characterized SUMO substrate. Furthermore, using TP53 as a substrate, we identify SUMO1, SUMO2 and Ubiquitin preferential interactors. Thus, SUMO-ID is a powerful tool that allows to study the consequences of SUMO-dependent interactions, and may further unravel the complexity of the ubiquitin code.
Mesh Terms:
Cell Line, Tumor, GTPase-Activating Proteins, HEK293 Cells, Humans, Promyelocytic Leukemia Protein, Protein Binding, Protein Interaction Mapping, Protein Interaction Maps, Protein Processing, Post-Translational, SUMO-1 Protein, Small Ubiquitin-Related Modifier Proteins, Sumoylation, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin
Cell Line, Tumor, GTPase-Activating Proteins, HEK293 Cells, Humans, Promyelocytic Leukemia Protein, Protein Binding, Protein Interaction Mapping, Protein Interaction Maps, Protein Processing, Post-Translational, SUMO-1 Protein, Small Ubiquitin-Related Modifier Proteins, Sumoylation, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin
Nat Commun
Date: Dec. 18, 2020
PubMed ID: 34795231
View in: Pubmed Google Scholar
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