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Related Experiment Video

Updated: May 8, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Global identification of modular cullin-RING ligase substrates.

Michael J Emanuele¹, Andrew E H Elia, Qikai Xu

¹Division of Genetics, Brigham and Women's Hospital, Boston, MA 02115, USA.

|October 4, 2011

Summary

Cullin-RING ligases (CRLs) regulate hundreds of proteins, including known and new substrates like NUSAP1. This reveals CRL ubiquitylation

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Area of Science:

Molecular Biology
Cellular Biology
Biochemistry

Background:

Cullin-RING ligases (CRLs) are the largest E3 ubiquitin ligase family in eukaryotes.
Identifying CRL substrates is crucial for understanding proteome regulation.

Purpose of the Study:

To identify CRL substrates and understand their role in cellular processes.
To investigate the regulation of NUSAP1 by CRLs.

Main Methods:

Genetic and pharmacologic Cullin inactivation.
Genetic (GPS) and proteomic (QUAINT) assays.
Analysis of protein stability and ubiquitylation.

Main Results:

Hundreds of CRL-regulated proteins identified, including known and novel substrates.
NUSAP1 identified as an SCF(Cyclin F) substrate during cell cycle (S and G2) and DNA damage.
Regulated substrates are enriched in protein interaction networks.

Conclusions:

CRL ubiquitylation plays a broad role in cellular biology.
Identified substrates provide key indicators of cellular physiology.