Abstract 1483 The phosphorylation-dependent activity of deubiquitinase USP7 in the Shoc2 signaling complex

The ERK1/2 signaling cascade is a tightly regulated fundamental signaling cascade. The Shoc2 scaffold protein plays a pivotal role in modulating ERK1/2 signaling by facilitating the assembly of signaling complexes and amplifying ERK1/2 activity. Our previous studies revealed a dynamic interaction between Shoc2 and the deubiquitinase USP7. USP7 binds to Shoc2 when the ERK1/2 pathway is activated and acts as a molecular switch to control the E3 ubiquitin ligase HUWE1 activity in the Shoc2 complex.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.110093
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 1483 The phosphorylation-dependent activity of deubiquitinase USP7 in the Shoc2 signaling complex

Patricia G. Wilson, Emilia Galperin, Seungjae Oh
Journal of Biological Chemistry
Ubiquitin and proteasome pathways
article

Abstract 1483 The phosphorylation-dependent activity of deubiquitinase USP7 in the Shoc2 signaling complex

Patricia G. Wilson, Emilia Galperin, Seungjae Oh
article en

Abstract

The ERK1/2 signaling cascade is a tightly regulated fundamental signaling cascade. The Shoc2 scaffold protein plays a pivotal role in modulating ERK1/2 signaling by facilitating the assembly of signaling complexes and amplifying ERK1/2 activity. Our previous studies revealed a dynamic interaction between Shoc2 and the deubiquitinase USP7. USP7 binds to Shoc2 when the ERK1/2 pathway is activated and acts as a molecular switch to control the E3 ubiquitin ligase HUWE1 activity in the Shoc2 complex.

Journal of Biological ChemistryVol. 301(5)
University of Kentucky (US)
U.S. Department of Defense, National Institutes of Health
Openalex Percentile: Top 88%
Ubiquitin and proteasome pathways
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