Sumo Sim Interaction
Sumo Sim Interaction - Related Videos
09:48
In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
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Cited by 13 •
2016
This work presents a protocol for liquid handling and sample introduction to a microchannel for in situ time-of-flight secondary ion mass spectrometry analysis of protein biomolecules in an aqueous solution.
06:23
Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
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Cited by 3 •
2019
SUMO is an essential and highly conserved, small ubiquitin-like modifier protein. In this protocol we are describing the use of a stress-tolerant recombinant SUMO-trapping protein (kmUTAG) to visualize native, untagged SUMO conjugates and their localization in a variety of cell types.
10:22
In Situ SIMS and IR Spectroscopy of Well-defined Surfaces Prepared by Soft Landing of Mass-selected Ions
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Cited by 4 •
2014
Soft landing of mass-selected ions onto surfaces is a powerful approach for the highly-controlled preparation of novel materials. Coupled with analysis by in situ secondary ion mass spectrometry (SIMS) and infrared reflection absorption spectroscopy (IRRAS), soft landing provides unprecedented insights into the interactions of well-defined species with surfaces.
09:56
In Situ Characterization of Shewanella oneidensis MR1 Biofilms by SALVI and ToF-SIMS
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Cited by 8 •
2017
This article presents a method for growing a biofilm for in situ time-of-flight secondary ion mass spectrometry for chemical mapping in its hydrated state, enabled by a microfluidic reactor, System for Analysis at the liquid Vacuum Interface. The Shewanella oneidensis MR-1 with green fluorescence protein was used as a model.
08:29
SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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Cited by 6 •
2019
Here, we present a protocol to enrich, isolate, identify, and characterize proteins modified by SUMO in vivo both from human hepatoma cells and liver tumors obtained from mouse models of hepatocellular carcinoma by using SUMO-binding entities (SUBEs).
FAQs
Hydrophobic residues in the SIM provide the principal contact with a complementary surface on SUMO. Acidic residues near the motif, or phosphorylation of nearby residues, can strengthen or regulate that association. These sequence features therefore help determine how effectively a partner recognizes SUMO and allow cellular conditions to modulate interaction-dependent signaling.
Because the association is noncovalent and reversible, partner proteins can engage with and disengage from SUMO as cellular conditions change. This differs from SUMO conjugation, which refers to attachment of SUMO rather than recognition through a binding motif. The distinction helps explain how cells can dynamically reorganize protein complexes and signaling responses.
Recognition can affect protein stability, subcellular localization, and assembly into larger molecular complexes. Consequently, a change in binding may alter where a protein acts, how long it persists, or which partners it joins. These effects connect a local molecular contact to broader regulation of cellular responses, particularly in processes that depend on coordinated protein organization.
The interaction contributes to several nuclear and stress-related processes, including transcription, DNA repair, chromatin regulation, and cellular stress responses. Its importance comes from coordinating protein recognition within pathways that require controlled assembly and localization. Studying these settings can reveal how cells organize nuclear signaling rather than treating protein interactions as isolated events.
Analysis of these interactions can clarify how proteins are recruited, retained, or redistributed during nuclear signaling. Researchers can relate binding behavior to changes in protein stability, localization, or complex assembly, then examine how those effects fit within transcription, DNA repair, chromatin regulation, or stress responses. This provides a molecular framework for interpreting coordinated cellular regulation.
Abnormal protein regulation can disrupt the cellular processes coordinated by SUMO-SIM recognition, including transcription, DNA repair, chromatin regulation, and stress responses. Investigating these interactions may therefore help researchers connect altered molecular recognition with broader cellular dysfunction. The approach is especially useful for understanding how disrupted nuclear signaling could contribute to disease-related regulatory abnormalities.