Modificomics: posttranslational modifications beyond protein phosphorylation and glycosylation
Joerg Reinders1, Albert Sickmann
1University of Wuerzburg, Proteomics Group, Pharmaceutical Biology, Julius-von-Sachs-Institute for Biosciences, Julius-von-Sachs-Platz 2, 97082 Wuerzburg, Germany.
Biomolecular Engineering
|April 10, 2007
Summary
This study addresses challenges in analyzing protein posttranslational modifications (PTMs). We offer guidelines for underrepresented PTMs to improve cellular process understanding.
Area of Science:
- Proteomics
- Molecular Biology
- Biochemistry
Background:
- Posttranslational modifications (PTMs) are crucial for cellular process regulation.
- PTMs significantly increase proteome complexity and alter protein properties.
- Standardized analysis methods exist for phosphorylation and glycosylation, but not all PTMs.
Purpose of the Study:
- To provide guidelines for analyzing underrepresented protein posttranslational modifications.
- To address the need for comprehensive analysis of diverse PTMs.
- To enhance the understanding of cellular processes regulated by PTMs.
Main Methods:
- Literature review of current PTM analysis techniques.
- Development of standardized protocols for underrepresented PTMs.
- Comparative analysis of different PTM detection and characterization methods.
Main Results:
- Established guidelines for analyzing specific underrepresented PTMs.
- Demonstrated the feasibility of comprehensive PTM analysis.
- Highlighted the importance of tailored solutions for complex PTMs.
Conclusions:
- Standardized guidelines are essential for advancing the study of underrepresented PTMs.
- Improved PTM analysis will deepen the understanding of cellular regulation.
- This work facilitates more thorough proteomic research.
Related Concept Videos
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.
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...
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...
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...
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...
01:25Protein Glycosylation
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...
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
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...