Related Experiment Video
Updated: Aug 12, 2026
09:36
Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
Published on: August 13, 2017
Non-classical protein Ser/Thr phosphatases: what are they for?
1Research School of Biological and Molecular Sciences, Oxford Brookes University, Headington, OX3 OBP, Oxford, UK. p0071233@brookes.ac.uk
Biochemistry. Biokhimiia
|April 3, 1999
Summary
This review covers the novel rdgC/Protein Phosphatase 5 (PP5) group, found across animals, fungi, and plants. We discuss their structure, cellular location, and potential roles in regulating cell functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein serine/threonine phosphatases are crucial regulators of cellular processes.
- A novel class of these enzymes, rdgC/Protein Phosphatase 5 (PP5), has been identified.
- This enzyme family is conserved across diverse eukaryotic organisms.
Purpose of the Study:
- To review the recently discovered rdgC/PP5 family of protein phosphatases.
- To elucidate the structural characteristics of rdgC/PP5.
- To explore the cellular localization and potential functions of rdgC/PP5.
Main Methods:
- Literature review of existing studies on rdgC/PP5.
- Comparative analysis of rdgC/PP5 sequences and structures.
- Bioinformatic analysis of predicted cellular localization and functional domains.
Main Results:
- The rdgC/PP5 family exhibits conserved structural features across species.
- rdgC/PP5 enzymes are found in various cellular compartments.
- Emerging evidence suggests diverse roles in cellular regulation.
Conclusions:
- The rdgC/PP5 phosphatases represent a significant, conserved enzyme group.
- Further research is needed to fully understand their specific functions.
- This review provides a foundation for future investigations into rdgC/PP5 biology.
Related Concept Videos
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...
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...
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...
01:22Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
01:27Transducer Mechanism: Enzyme-Linked Receptors
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include: