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Related Concept Videos

Allosteric Regulation01:08

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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...
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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.
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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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Related Experiment Video

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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Allosteric substrate switching in a voltage-sensing lipid phosphatase.

Sasha S Grimm1, Ehud Y Isacoff1,2,3,4

  • 1Biophysics Graduate Group, University of California, Berkeley, California, USA.

Nature Chemical Biology
|February 16, 2016
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Summary

The voltage-sensing phosphatase (Ci-VSP) has two active states, controlled by voltage-sensing domain movements. This dual-state allostery precisely regulates phosphoinositide signaling lipids (PIPs) in response to voltage changes.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Allosteric regulation is crucial for controlling enzyme activity.
  • Voltage-sensing phosphatases (VSPs) modulate phosphoinositide signaling lipids (PIPs).
  • The specific mechanisms of VSP allosteric control are not fully understood.

Purpose of the Study:

  • To investigate the allosteric control of Ciona intestinalis VSP (Ci-VSP) activity.
  • To elucidate the relationship between voltage-sensing domain (VSD) conformation and enzyme substrate specificity.
  • To understand how voltage dynamically shapes PIP concentrations.

Main Methods:

  • Utilized fast fluorescence resonance energy transfer (FRET) reporters to monitor PIP levels and enzyme activity.
  • Employed voltage-clamp fluorometry to track VSD conformational changes.
  • Correlated VSD movements with changes in Ci-VSP substrate preference.

Main Results:

  • Ci-VSP exhibits two sequential active states with distinct PIP substrate specificities.
  • An initial VSD motion transitions Ci-VSP to a PIP3-preferring state.
  • Full VSD activation shifts Ci-VSP to a PIP2-preferring state.
  • These transitions are allosterically controlled by VSD conformations.

Conclusions:

  • Ci-VSP's two-step allosteric control allows voltage to dynamically regulate PIP concentrations.
  • This mechanism provides insight into the modulation of PIP-regulated cellular processes.
  • The findings reveal a novel mechanism for voltage-dependent modulation of signaling pathways.