Sumoylated Proteome
Sumoylated Proteome - Related Videos
06:00
SUMOylation Assay: An In Vitro Technique to Detect the SUMOylation Status of Substrate Proteins by Immunoblotting
0 Views •
2025
This video demonstrates the in vitro method for SUMOylation of substrate proteins using a sequential enzyme cascade. Further, the SUMOylated status of the protein is identified using the electrophoresis and immunoblotting technique.
09:40
In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
0 Views •
Cited by 2 •
2017
Small ubiquitin-related modifier (SUMO) family proteins are conjugated to the lysine residues of target proteins to regulate various cellular processes. This paper describes a protocol for the detection of retinoblastoma (Rb) protein SUMOylation under endogenous and exogenous conditions in human cells.
09:29
Skeletal Muscle Gender Dimorphism from Proteomics
0 Views •
Cited by 4 •
2011
A straight-forward set of methods to isolate and determine the identity of the most abundant proteins expressed in skeletal muscle. About 800 spots are discerned on a two-dimensional gel from 10 mg muscle; this allows for the determination of gender-specific protein expression. These methods will give equivalent results in most tissues.
09:20
Proteomic Sample Preparation from Formalin Fixed and Paraffin Embedded Tissue
0 Views •
Cited by 50 •
2013
Archival formalin fixed and paraffin embedded (FFPE) clinical samples are valuable material for investigation of diseases. Here we demonstrate a sample preparation workflow allowing in-depth proteomic analysis of microdissected FFPE tissue.
14:23
Bottom-up and Shotgun Proteomics to Identify a Comprehensive Cochlear Proteome
0 Views •
Cited by 6 •
2014
Proteome analysis of the cochlear sensory epithelium can be challenging due to its small size and because membrane proteins are difficult to isolate and identify. Both membrane and soluble proteins can be identified by combining multiple preparative methods and separation techniques along with high-resolution mass spectrometry.
FAQs
SUMO modification proceeds through an enzyme relay rather than direct spontaneous attachment. The E1 enzyme activates SUMO, Ubc9 serves as the E2 conjugating enzyme that receives it, and E3 ligases assist transfer to target proteins, often at lysine residues. This coordinated arrangement helps connect SUMO attachment with regulated protein targeting and cellular responses.
Sentrin-specific proteases, or SENPs, remove SUMO from modified proteins, counterbalancing the enzymes that attach it. Their activity makes sumoylation reversible, so a measured modification profile reflects both conjugation and removal. This reversibility allows cellular SUMO regulation to change with conditions and helps explain why modified-protein abundance can vary across experiments.
SUMO attachment can influence several functional properties of a protein, including its localization within the cell, interaction partners, stability, and participation in DNA repair or transcription. Consequently, a change in the sumoylated proteome may indicate altered protein regulation even when total protein levels are not the primary measurement, especially during stress responses.
A typical workflow enriches SUMO-modified proteins or peptides through affinity-based methods and then identifies them by mass spectrometry. The resulting measurements reveal which proteins carry SUMO and can be compared between cellular conditions. This combination connects modification-site or protein-identification data with broader biochemical interpretation of regulated pathways.
Researchers compare affinity-enriched, mass-spectrometry-derived profiles from different cellular states to identify changes in SUMO-modified proteins. Such comparisons can reveal condition-responsive pathways rather than only a static list of targets. Interpreting the differences requires attention to the dynamic balance between SUMO attachment and SENP-mediated removal, because both processes shape the observed profile.
This analysis can identify regulatory pathways associated with transcription, DNA repair, protein localization, stability, interactions, and stress responses. In biochemistry, it provides a systems-level view of how covalent modification reorganizes protein function. Comparing profiles may also highlight disease-associated changes, helping connect altered SUMO regulation with broader cellular or pathological processes.