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Related Experiment Video

Updated: Jun 2, 2026

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
08:29

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

SUMO and its role in human diseases.

Kevin D Sarge1, Ok-Kyong Park-Sarge

  • 1Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA.

International Review of Cell and Molecular Biology
|April 13, 2011
PubMed
Summary

Sumoylation, a protein modification, impacts proteins linked to diseases like Alzheimer's and Parkinson's. New research shows sumoylation of amyloid precursor protein (APP) and lamin A is crucial for health.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Regulation

Background:

  • Protein modification through covalent attachment of small ubiquition-like modifier (SUMO) polypeptides, known as sumoylation, is a key regulatory mechanism.
  • Sumoylation influences the function of numerous proteins, many of which are implicated in significant human diseases such as cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis.

Purpose of the Study:

  • To identify and investigate the role of sumoylation in human disease-associated proteins.
  • To explore the functional implications of sumoylation on amyloid precursor protein (APP) and lamin A.

Main Methods:

  • Literature review of recent studies.
  • Analysis of protein sumoylation.

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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Published on: January 29, 2018

  • Investigation of disease-associated protein modifications.
  • Main Results:

    • Two additional human disease-associated proteins, amyloid precursor protein (APP) and lamin A, have been identified as sumoylated.
    • APP sumoylation was found to modulate Aβ peptide levels, indicating a potential role in Alzheimer's disease pathogenesis.
    • Decreased lamin A sumoylation, resulting from mutations near its SUMO site, is implicated in familial dilated cardiomyopathy.

    Conclusions:

    • Sumoylation is a critical regulatory process with implications for a range of human diseases.
    • Dysregulation of APP and lamin A sumoylation contributes to the development of Alzheimer's disease and familial dilated cardiomyopathy, respectively.