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Related Concept Videos

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Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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Related Experiment Video

Updated: Jul 13, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

SUMO-1: Ubiquitin gains weight.

P R Johnson, M Hochstrasser

    Trends in Cell Biology
    |August 22, 2007
    PubMed
    Summary

    The ubiquitin system modifies proteins, impacting proteasome degradation and other cellular processes. New research shows ubiquitin-like proteins, such as SUMO-1, also modify proteins, influencing nucleocytoplasmic trafficking and revealing broader biological roles.

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • The ubiquitin polypeptide is a highly conserved protein involved in covalent modification of other proteins.
    • Ubiquitin modification is known to facilitate substrate degradation by the proteasome and regulate proteins through proteasome-independent pathways.
    • Emerging evidence indicates that proteins with distant similarity to ubiquitin can also be attached to other proteins.

    Purpose of the Study:

    • To explore the broader roles of the 'ubiquitin system' in cell biology.
    • To investigate the functional consequences of modifications by ubiquitin-like proteins.
    • To understand the regulatory and mechanistic aspects of these modifications.

    Main Methods:

    • Literature review of recent findings on ubiquitin and ubiquitin-like proteins.

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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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    Last Updated: Jul 13, 2026

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    In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

    Published on: January 29, 2018

    In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
    09:40

    In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

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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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  • Analysis of studies on SUMO-1 modification.
  • Examination of protein trafficking and nuclear pore complex interactions.

    • Main Results:

    • Ubiquitin-like proteins, exemplified by SUMO-1, can be attached to specific proteins.
    • SUMO-1 modification has been shown to target a protein involved in nucleocytoplasmic trafficking to the nuclear pore complex.
    • The consequences of most ubiquitin-like protein modifications remain largely uncharacterized.

    Conclusions:

    • The 'ubiquitin system' exerts a wider influence on cell biology than previously understood.
    • Ubiquitin-like protein modifications, including SUMO-1, play significant roles in cellular regulation, such as nucleocytoplasmic transport.
    • Further research is needed to elucidate the diverse regulatory mechanisms and functional outcomes of these modifications.