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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Oct 12, 2025

SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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Identification of proximal SUMO-dependent interactors using SUMO-ID.

Orhi Barroso-Gomila1, Fredrik Trulsson2, Veronica Muratore1

  • 1Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.

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|November 19, 2021
PubMed
Summary

SUMO-ID is a new technology that identifies proteins interacting with SUMO-modified proteins. This tool helps researchers understand the complex roles of SUMOylation in cellular processes and the ubiquitin code.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Posttranslational modifications by the ubiquitin family, such as SUMOylation, are dynamic and reversible, posing research challenges.
  • Understanding SUMO-dependent interactions is crucial for deciphering cellular signaling pathways.

Purpose of the Study:

  • To develop a novel technology, SUMO-ID, for identifying SUMO-dependent protein interactors.
  • To investigate the SUMOylation-dependent interactomes of specific proteins like PML and RANGAP1.

Main Methods:

  • SUMO-ID merges proximity biotinylation using TurboID with protein-fragment complementation.
  • An optimized split-TurboID system was developed and validated for SUMO interaction-dependent labeling.

Main Results:

  • SUMO-ID successfully identified SUMO-dependent interactors proximal to PML and RANGAP1.
  • Interactors of PML were enriched in SUMO Interacting Motifs and involved in transcription, DNA damage, and stress response.
  • SUMO-ID also revealed interactors of SUMOylated SALL1 and identified preferential interactors for SUMO1, SUMO2, and Ubiquitin using TP53.

Conclusions:

  • SUMO-ID is a powerful tool for studying SUMO-dependent interactions and their functional consequences.
  • This technology can help unravel the complexity of the ubiquitin code and SUMOylation networks.