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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Structural basis for protein phosphatase 1 regulation and specificity.
Wolfgang Peti1, Angus C Nairn, Rebecca Page
1Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA. wolfgang_peti@brown.edu
The FEBS Journal
|January 31, 2012
Summary
Protein Phosphatase 1 (PP1) controls key cell functions but needs regulatory proteins for specificity. Recent structural studies reveal how these complexes achieve molecular regulation and substrate targeting.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Serine/threonine protein phosphatase 1 (PP1) is a crucial enzyme regulating fundamental cellular processes.
- The catalytic subunit of PP1 lacks intrinsic substrate specificity.
- Specificity is conferred by over 200 regulatory proteins, forming holoenzyme complexes.
Purpose of the Study:
- To review recent structural studies of PP1 holoenzyme complexes.
- To summarize new insights into the molecular mechanisms of PP1 regulation.
- To elucidate the basis of PP1 substrate specificity.
Main Methods:
- Structural biology techniques (e.g., X-ray crystallography, cryo-EM).
- Biochemical assays to study enzyme activity and substrate interactions.
- Bioinformatic analysis of PP1-regulatory protein complexes.
Main Results:
- Advances in structural determination of various PP1 holoenzymes.
- Identification of key structural features mediating PP1-regulator interactions.
- Elucidation of how regulatory proteins dictate PP1 substrate targeting and activity.
Conclusions:
- Structural insights are critical for understanding PP1 function.
- PP1 regulation is achieved through intricate protein-protein interactions within holoenzymes.
- Future research directions in PP1 structural biology and its role in cellular signaling.
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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...
01:02Phosphorylation
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
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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...
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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.