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Related Concept Videos

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...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying 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...

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Pseudokinases-remnants of evolution or key allosteric regulators?

Elton Zeqiraj1, Daan M F van Aalten

  • 1Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Room 1090, Toronto, Ontario M5G 1X5, Canada. zeqiraj@lunenfeld.ca

Current Opinion in Structural Biology
|November 16, 2010
PubMed
Summary

Pseudokinases, or inactive protein kinases, are now understood to play crucial roles in cell signaling. Recent studies reveal their function as signal integrators and activators of other kinases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein kinases are central to cellular signal transduction networks.
  • Kinase activity often involves mutual activation through phosphorylation.
  • Some kinases, termed pseudokinases, lack phosphoryl group transfer ability due to degraded catalytic motifs.

Purpose of the Study:

  • To investigate the biological roles and evolutionary significance of pseudokinases.
  • To elucidate the molecular basis of pseudokinase inactivity.
  • To understand how pseudokinases contribute to cellular signal transduction.

Main Methods:

  • Sequence homology analysis to predict kinase catalytic activity.
  • Structure-function studies to determine molecular determinants of inactivity.
  • Analysis of pseudokinase roles in cellular signaling pathways.

Main Results:

  • Identified molecular determinants responsible for pseudokinase inactivity.
  • Uncovered novel biological functions for pseudokinases.
  • Demonstrated that pseudokinases function as signal transducers by assembling signaling networks.
  • Revealed pseudokinases can act as allosteric activators of active protein kinases.

Conclusions:

  • Pseudokinases are not merely inactive enzymes but possess critical signaling functions.
  • Understanding pseudokinases provides insights into the evolution of the human kinome.
  • Pseudokinases integrate signals and modulate kinase activity, expanding the complexity of cellular communication.