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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
Published on: June 14, 2017
Post-translational modification of cardiac proteasomes: functional delineation enabled by proteomics
Sarah B Scruggs1, Nobel C Zong, Ding Wang
1Division of Cardiology, Department of Physiology, University of California, Los Angeles, USA.
Summary
Post-translational modifications (PTMs) on proteasomes create functional subpopulations in cardiac muscle. Advanced proteomics now enable detailed analysis of these crucial PTMs in heart health and disease.
Area of Science:
- Molecular Biology
- Biochemistry
- Proteomics
Background:
- Proteasomes are essential for protein homeostasis, existing as diverse subpopulations in cardiac muscle.
- Post-translational modifications (PTMs) significantly influence proteasome function, assembly, and localization.
- Previous methods for PTM analysis lacked site specificity and quantitative capabilities.
Purpose of the Study:
- To discuss the role of PTMs in cardiac proteasome function during physiological and pathophysiological states.
- To present an advanced proteomic workflow for comprehensive PTM identification and quantification in cardiac proteasomes.
Main Methods:
- Review of the importance of PTMs in cardiac proteasome biology.
- Implementation of a state-of-the-art proteomic workflow.
- Site-specific and quantitative analysis of PTMs on cardiac proteasomes.
Main Results:
- PTMs critically modulate various aspects of proteasome activity and regulation in the heart.
- Advanced proteomic techniques overcome limitations of classical PTM identification methods.
- The presented workflow allows for large-scale, multi-PTM analysis with high precision.
Conclusions:
- PTMs are key determinants of cardiac proteasome heterogeneity and function.
- The developed proteomic approach provides novel insights into cardiac proteasome regulation.
- This methodology is vital for understanding cardiac physiology and developing therapeutic strategies.
Related Concept Videos
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Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
02:18The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
01:13The Proteasome
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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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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.
02:11Proteins: From Genes to Degradation
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