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Related Experiment Video

Updated: Jan 13, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.

Richard M Searfoss¹, Benjamin A Garcia¹, Zongtao Lin²

¹Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA.

Chembiochem : a European Journal of Chemical Biology

|October 28, 2025

Summary

This summary is machine-generated.

Arginylation, a protein modification marking proteins for degradation, is crucial for mammalian systems. This review summarizes methods developed over six decades to identify and study arginylation substrates.

Keywords:

ATE1 arginylation cDNA screening proteomics radiolabeling

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Last Updated: Jan 13, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

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Published on: August 7, 2021

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

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Published on: February 27, 2020

Identification of Kinase-substrate Pairs Using High Throughput Screening

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Published on: August 29, 2015

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Arginylation is a post-translational modification involving the addition of arginine.
It plays a critical role in protein degradation, stability, and function in mammals.
Loss of arginylation enzymes is embryonically lethal, highlighting its essential nature.

Purpose of the Study:

To provide a comprehensive summary of all methodologies used for discovering and studying arginylation.
To consolidate knowledge on the diverse approaches employed over six decades.

Main Methods:

Review of historical and contemporary scientific literature.
Analysis of various experimental strategies applied to substrate identification.
Categorization of techniques based on their application to arginylation research.

Main Results:

Arginylation substrate discovery has evolved significantly since the 1960s.
Diverse creative approaches have been necessary due to the challenges in characterizing this modification.
A growing library of substrates has been identified through various applications.

Conclusions:

Understanding arginylation requires a diverse toolkit of discovery methods.
Continued development of novel approaches will further expand the known substrates and functions of arginylation.
This review serves as a resource for researchers investigating protein degradation pathways.