Analysis of posttranslational modifications exemplified using protein kinase A

With the completion of the major genome projects, one focus in biomedical research has shifted from the analysis of the rather static genome to the highly dynamic proteome. The sequencing of whole genomes did not lead to much anticipated insights into disease mechanisms; however, it paved the way fo...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2006-12, Vol.1764 (12), p.1788-1800
Main Authors: Gesellchen, Frank, Bertinetti, Oliver, Herberg, Friedrich W.
Format: Article
Language:English
Subjects:
Acylation
Amino Acid Sequence
Asparagine - metabolism
cAMP-dependent protein kinase
Cyclic AMP-Dependent Protein Kinases - chemistry
Cyclic AMP-Dependent Protein Kinases - metabolism
Deamidation
Mass spectrometry
Models, Molecular
Molecular Sequence Data
Myristic Acid - metabolism
Myristoylation
Phosphorylation
Protein Processing, Post-Translational
Proteomics - methods
Tandem Mass Spectrometry
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Summary:With the completion of the major genome projects, one focus in biomedical research has shifted from the analysis of the rather static genome to the highly dynamic proteome. The sequencing of whole genomes did not lead to much anticipated insights into disease mechanisms; however, it paved the way for proteomics by providing the databases for protein identification by peptide mass fingerprints. The relative protein distribution within a cell or tissue is subject to change upon external and internal stimuli. Signal transduction events extend beyond a simple change in protein levels; rather they are governed by posttranslational modifications (PTMs), which provide a quick and efficient way to modulate cellular signals. Because most PTMs change the mass of a protein, they are amenable to analysis by mass spectrometry. Their investigation adds a level of functionality to proteomics, which can be expected to greatly aid in the understanding of the complex cellular machinery involved in signal transduction, metabolism, differentiation or in disease. This review provides an overview on posttranslational modifications exemplified on the model system cAMP-dependent protein kinase. Strategies for detection of selected PTMs are described and discussed in the context of protein kinase function.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/j.bbapap.2006.10.001