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Related Experiment Video

Updated: Apr 21, 2026

Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

Published on: September 20, 2011

Selective allosteric coupling in core chemotaxis signaling complexes.

Mingshan Li¹, Gerald L Hazelbauer²

¹Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211.

Proceedings of the National Academy of Sciences of the United States of America

|October 29, 2014

Summary

This summary is machine-generated.

Bacterial chemotaxis relies on allosteric interactions within signaling complexes. This study reveals how receptor dimers selectively inhibit kinase activity, enabling signal amplification for directed bacterial movement.

Keywords:

Nanodiscs allosteric coupling bacterial chemotaxis histidine kinases transmembrane receptors

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Imaging G Protein-coupled Receptor-mediated Chemotaxis and its Signaling Events in Neutrophil-like HL60 Cells

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Last Updated: Apr 21, 2026

Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

Published on: September 20, 2011

Assessment of Dictyostelium discoideum Response to Acute Mechanical Stimulation

Assessment of Dictyostelium discoideum Response to Acute Mechanical Stimulation

Published on: November 9, 2017

Imaging G Protein-coupled Receptor-mediated Chemotaxis and its Signaling Events in Neutrophil-like HL60 Cells

Imaging G Protein-coupled Receptor-mediated Chemotaxis and its Signaling Events in Neutrophil-like HL60 Cells

Published on: September 14, 2016

Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

Bacterial chemotaxis involves complex signaling pathways to sense chemical gradients.
Allosteric interactions within signaling complexes are crucial for cooperativity and amplification.
The precise mechanisms of allostery in chemotaxis signaling remain incompletely understood.

Purpose of the Study:

To investigate allosteric interactions in bacterial chemotaxis core signaling complexes.
To determine how ligand occupancy influences kinase inhibition within these complexes.
To elucidate the role of structural asymmetry in mediating allosteric communication.

Main Methods:

Reconstitution of core signaling complexes using two chemoreceptor species in Nanodiscs.
Isolation of individual complexes for detailed analysis.
Assessment of allosteric coupling and kinase inhibition as a function of ligand binding.

Main Results:

Neighboring receptor dimers exhibit allosteric coupling affecting ligand affinity.
Only one receptor dimer within a trimer effectively inhibits kinase activity.
Kinase protomers are allosterically coupled, allowing inhibition to propagate across dimer interfaces.

Conclusions:

Selective allosteric coupling in receptor dimers mediates kinase inhibition, consistent with structural asymmetry.
Propagated kinase inhibition across dimer interfaces facilitates signal amplification in bacterial chemotaxis.
These findings provide insights into the molecular basis of highly sensitive chemotactic responses.