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Cbl interacts with multiple E2s in vitro and in cells.

Mariya S Liyasova¹, Ke Ma¹, Donna Voeller¹

¹Women's Malignancy Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.

|May 24, 2019

Summary

This summary is machine-generated.

Cbl proteins regulate receptor tyrosine kinases (RTKs) via ubiquitination. Multiple ubiquitin-conjugating enzymes (E2s) interact with Cbl, modulating its E3 ligase activity and influencing RTK ubiquitination in cells.

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In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Area of Science:

Cellular biology
Molecular biology
Biochemistry

Background:

Cbl proteins are RING finger (RF) ubiquitin ligases (E3s) that negatively regulate receptor tyrosine kinases (RTKs) like EGFR and MET through ubiquitination and degradation.
Loss of Cbl function is linked to malignant transformation due to elevated RTK activity.

Purpose of the Study:

To investigate the roles of various ubiquitin-conjugating enzymes (E2s) in Cbl-mediated ubiquitination of RTKs.
To determine how different E2s affect Cbl E3 ligase activity and ubiquitin chain formation.

Main Methods:

In vitro E3 assays and yeast two-hybrid screens were employed.
Ubiquitination assays were performed using Cbl, E2s, and substrates like EGFR and SYK.
Cellular ubiquitination of EGFR was assessed.

Main Results:

Several E2s, including Ube2d, Ube2e, Ube2n/2v1, and Ube2w, were found to catalyze Cbl autoubiquitination.
Ube2d2, Ube2e1, and Ube2n/2v1 mediated Cbl-dependent ubiquitination of EGFR and SYK.
Phosphorylation of Cbl by Src enhanced its E3 activity.
Specific E2s dictated ubiquitin chain linkage types (K48, K63, or monoubiquitination).
Ube2d, Ube2e, and Ube2n/2v1 families contributed to EGFR ubiquitination in cells.

Conclusions:

Multiple E2 enzymes can interact with Cbl proteins.
These E2s modulate Cbl E3 ligase activity both in vitro and within cellular contexts.
Understanding these E2-Cbl interactions is crucial for comprehending RTK regulation and potential therapeutic strategies.