Related Experiment Video
Updated: Apr 30, 2026
12:11
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
8.1K
Global analysis of posttranslational protein arginylation
Catherine C L Wong1, Tao Xu, Reena Rai
1The Scripps Research Institute, LaJolla, California, United States of America.
Plos Biology
|September 28, 2007
Summary
Posttranslational arginylation, a key process in development, was globally analyzed. Researchers identified 43 arginylated proteins, revealing its broad impact on cell structure and metabolism.
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- Posttranslational arginylation is essential for embryogenesis, cardiovascular development, and angiogenesis.
- The precise molecular functions and in vivo targets of arginylation remain largely uncharacterized.
Purpose of the Study:
- To conduct a global analysis of protein arginylation in vivo.
- To identify specific proteins and sites modified by arginylation.
- To elucidate the physiological systems and pathways affected by this modification.
Main Methods:
- Global proteomic analysis to identify arginylated proteins.
- Mass spectrometry-based identification of arginylation sites on proteins.
- Bioinformatic analysis to determine affected physiological systems and pathways.
Main Results:
- Identified 43 proteins that are arginylated in vivo at specific sites.
- Demonstrated that arginylation can occur on any N-terminally exposed residue, not limited by specific sequences.
- Revealed preferential arginylation of proteins involved in the cytoskeleton and primary metabolic pathways.
Conclusions:
- Protein arginylation is a widespread regulatory mechanism impacting protein structure and function.
- Arginylation plays a significant role in cellular metabolism and embryonic development.
- This study provides a foundation for understanding the broader biological roles of arginylation.
Related Concept Videos
02:04Covalently Linked Protein Regulators
8.2K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
8.2K
01:25Protein Glycosylation
8.4K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
8.4K
01:26Protein Modifications in the RER
5.6K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.6K