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Updated: Jul 18, 2026
10:07
Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Analysis of posttranslational modifications exemplified using protein kinase A
Frank Gesellchen1, Oliver Bertinetti, Friedrich W Herberg
1Universität Kassel, FB 18 Naturwissenschaften, Abt. Biochemie, Heinrich-Plett-Str. 40, 34132 Kassel, Germany.
Biochimica Et Biophysica Acta
|November 14, 2006
Summary
Proteomics research now focuses on dynamic proteomes, not just static genomes. Posttranslational modifications (PTMs) are key to understanding cellular signals and disease mechanisms, detectable via mass spectrometry.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Genome projects shifted research focus to the dynamic proteome.
- Protein identification is now database-driven via peptide mass fingerprints.
- Posttranslational modifications (PTMs) are crucial for modulating cellular signals.
Purpose of the Study:
- To provide an overview of PTMs in proteomics.
- To illustrate PTM analysis using cAMP-dependent protein kinase as a model.
- To discuss strategies for detecting PTMs and their role in protein kinase function.
Main Methods:
- Mass spectrometry for PTM detection due to mass alterations.
- Utilizing peptide mass fingerprints for protein identification.
- Reviewing established and novel PTM detection strategies.
Main Results:
- PTMs offer functional insights beyond protein levels.
- Mass spectrometry is amenable to PTM analysis.
- Understanding PTMs aids in deciphering complex cellular processes.
Conclusions:
- PTMs are essential for dynamic cellular regulation and signal transduction.
- Proteomics, enhanced by PTM analysis, is vital for understanding disease.
- Further investigation of PTMs will illuminate cellular machinery and kinase function.
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