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Related Experiment Video

Updated: Feb 9, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Regulating the human HECT E3 ligases.

Jasper Sluimer¹, Ben Distel^2,3

¹Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.

Cellular and Molecular Life Sciences : CMLS

|June 3, 2018

Summary

This summary is machine-generated.

HECT E3 ligases control cell pathways through ubiquitination. Their activity and specificity are tightly regulated by various mechanisms, crucial for preventing disease and enabling therapeutic strategies.

Keywords:

Activity regulation HECT E3 ligase Intramolecular interaction Oligomerization Post-translational modification Substrate recruitment Ubiquitination

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Last Updated: Feb 9, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function

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Published on: May 14, 2021

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

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Published on: December 5, 2019

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Ubiquitination by HECT E3 ligases is vital for cellular processes.
Dysregulation of HECT E3 ligases is implicated in various diseases.
Understanding HECT E3 regulation is key to cellular health and disease intervention.

Purpose of the Study:

To summarize regulatory mechanisms controlling HECT E3 ligase activity and substrate specificity.
To highlight the importance of these mechanisms in physiological and pathological contexts.
To explore potential therapeutic applications based on HECT E3 regulation.

Main Methods:

Review of existing literature on HECT E3 ligase regulation.
Analysis of protein-protein interactions, post-translational modifications, and calcium ion binding.
Examination of mechanisms controlling E2 recruitment and HECT E3 oligomerization.

Main Results:

Substrate specificity is often dictated by adaptor proteins interacting with HECT E3 N-terminal domains.
HECT E3 activity is regulated via E2 recruitment, oligomerization, and inhibitory conformations.
HECT E3 ligases can be modulated to control ubiquitin polymer types.

Conclusions:

Diverse regulatory mechanisms ensure precise control of HECT E3 ligase function.
Understanding these mechanisms offers therapeutic targets for diseases linked to HECT E3 dysregulation.
Modulating HECT E3 activity and specificity presents new avenues for treatment.