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Related Experiment Video

Updated: May 2, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Tomosyn interacts with the SUMO E3 ligase PIASγ.

Cornelia J Geerts¹, Linda Jacobsen¹, Rhea van de Bospoort¹

¹Department of Functional Genomics, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University, Amsterdam, Netherlands.

|March 12, 2014

Summary

Tomosyn-1 interacts with PIASγ, a SUMO E3 ligase, revealing a new mechanism for regulating neurotransmission. This SUMOylation process adapts synaptic strength to neuronal activity.

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Area of Science:

Neuroscience
Molecular Biology
Cell Biology

Background:

Small Ubiquitin-like MOdifier (SUMO) conjugation regulates critical neuronal functions like synaptogenesis and synaptic plasticity.
Tomosyn-1, a syntaxin-binding protein 5 (STXPB5), is a key regulator of neurotransmission and one of the few identified neuronal SUMO substrate proteins.

Purpose of the Study:

To identify novel protein interactions of tomosyn-1.
To elucidate the mechanism by which tomosyn-1 is SUMOylated in neurons.
To understand how SUMOylation of tomosyn-1 impacts synaptic function.

Main Methods:

Yeast two-hybrid screening to identify protein interactors.
Co-immunoprecipitation assays to confirm protein interactions.
Expression of full-length proteins in HEK293T cells.

Main Results:

Tomosyn-1 was found to interact with the SUMO E3 ligase PIASγ (PIAS4/ZMIZ6).
The interaction occurred between the C-terminus of tomosyn-1 and the N-terminus of PIASγ.
Tomosyn-1 was preferentially modified by the SUMO-2/3 isoform in a PIASγ-dependent manner.

Conclusions:

A novel interaction between tomosyn-1 and PIASγ was discovered, mediated by specific protein domains.
PIASγ-dependent SUMO-2/3 modification of tomosyn-1 provides a new regulatory mechanism for synaptic strength.
This mechanism allows secretory strength to adapt to the dynamic synaptic environment, impacting neuronal function.