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Phospho-mimetic CheV interacts with a subset of chemoreceptors
Phospho-mimetic CheV interacts with a subset of chemoreceptors
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Phospho-mimetic CheV interacts with a subset of chemoreceptors
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Phospho-mimetic CheV interacts with a subset of chemoreceptors
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Phospho-mimetic CheV interacts with a subset of chemoreceptors
Phospho-mimetic CheV interacts with a subset of chemoreceptors
Journal Article

Phospho-mimetic CheV interacts with a subset of chemoreceptors

2025
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Overview
CheV is one of the least understood chemosensory signaling proteins. Our demonstration that CheV interacts only with certain chemoreceptors offers fundamental new insights. These findings, combined with the observation that CheV is present in bacteria with numerous chemoreceptors, suggest that CheV plays a role in coordinating chemotactic outputs in complex chemosensory systems. Understanding the mechanisms by which chemotactic responses are defined in bacteria with a high number of chemoreceptors is a major research priority in the field of chemotaxis. While previous studies, including this one, show that the ability to be phosphorylated is crucial for CheV function, the molecular consequences of CheV phosphorylation have remained unclear. Our discovery that phosphorylation is essential for CheV binding to certain chemoreceptors fills in this critical gap in understanding the molecular mechanism of CheV. This study is likely to inspire further research into CheV function in other bacteria using similar approaches.