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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Protein Kinases and Phosphatases02:54

Protein 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 and Phosphatases02:54

Protein 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...
Phosphorylation01:02

Phosphorylation

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...
Phosphorylation01:02

Phosphorylation

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Distributivity and processivity in multisite phosphorylation can be distinguished through steady-state invariants.

Jeremy Gunawardena1

  • 1Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA.

Biophysical Journal
|August 21, 2007
PubMed
Summary

Mathematical analysis reveals steady-state invariants for studying multisite protein phosphorylation. These invariants help determine enzyme mechanisms and processivity from steady-state measurements, aiding cellular regulation research.

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Area of Science:

  • Biochemistry and Molecular Biology
  • Systems Biology
  • Enzymology

Background:

  • Multisite protein phosphorylation and dephosphorylation are crucial cellular regulatory processes.
  • Studying the system properties of these mechanisms in vivo and in vitro presents significant challenges.
  • Understanding enzyme kinetics and mechanisms is vital for deciphering cellular signaling pathways.

Purpose of the Study:

  • To develop a mathematical framework for analyzing multisite protein phosphorylation and dephosphorylation.
  • To demonstrate how steady-state invariants can elucidate enzyme mechanisms and substrate modification.
  • To investigate the impact of enzyme processivity on these steady-state properties.

Main Methods:

  • Mathematical analysis of multisite phosphorylation/dephosphorylation systems.
  • Derivation and application of steady-state invariants.
  • Analysis of enzyme action, distinguishing between distributive and processive mechanisms.

Main Results:

  • Steady-state invariants were identified that allow determination of kinase or phosphatase mechanisms from steady-state measurements.
  • These invariants are applicable when enzymes act distributively (nonprocessively).
  • For two-site substrates, enzyme processivity can be estimated by observing changes in the derived invariant.

Conclusions:

  • Steady-state invariants provide a powerful tool for dissecting the mechanisms of protein phosphorylation and dephosphorylation.
  • The degree of enzyme processivity significantly influences these invariants, offering a way to quantify it.
  • Further experimental and theoretical work is needed to extend these findings to more complex biological systems.