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Updated: Jun 10, 2026
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Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
Published on: May 18, 2017
Protein PTMs: post-translational modifications or pesky trouble makers?
Ralph A Bradshaw1, Katalin F Medzihradszky, Robert J Chalkley
1NCRR Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, UCSF, San Francisco, CA 94158-2517, USA.
Journal of Mass Spectrometry : JMS
|July 17, 2010
Summary
Mass spectrometry is key for studying protein post-translational modifications. Challenges in modification site assignment and data reliability hinder proteomic research progress.
Area of Science:
- Proteomics
- Mass Spectrometry
- Post-Translational Modifications
Background:
- Protein post-translational modifications (PTMs) are crucial for cellular functions.
- Mass spectrometry (MS) is a primary technology for PTM analysis in proteomics.
Purpose of the Study:
- To review the current capabilities and challenges in PTM analysis using MS.
- To address issues concerning modification site assignment and data reliability.
Main Methods:
- This perspective synthesizes current literature and expert knowledge on PTM analysis via MS.
- It critically evaluates the state-of-the-art in identifying and localizing PTMs.
Main Results:
- Significant advancements have been made in PTM detection.
- However, reliable modification site assignment remains a major challenge.
- The reliability of published PTM data varies, impacting downstream research.
Conclusions:
- Improving the reliability of PTM site assignment is critical for advancing proteomic research.
- Standardized validation methods and transparent reporting are needed.
- Addressing data quality issues will enhance the utility of MS-based PTM analysis.
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02:04Covalently Linked Protein Regulators
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.
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
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01:26Protein Modifications in the RER
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 sequences.
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01:30Point and Frameshift Mutations
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