Signal integration in chemoreceptor complexes

Moriah Koler, John S. Parkinson, Ady Vaknin

Research output: Contribution to journalArticlepeer-review

Abstract

Motile bacteria use large receptor arrays to detect chemical and physical stimuli in their environment, process this complex information, and accordingly bias their swimming in a direction they deem favorable. The chemoreceptor molecules form tripod-like trimers of receptor dimers through direct contacts between their cytoplasmic tips. A pair of trimers, together with a dedicated kinase enzyme, form a core signaling complex. Hundreds of core complexes network to form extended arrays. While considerable progress has been made in revealing the hierarchical structure of the array, the molecular properties underlying signal processing in these structures remain largely unclear. Here we analyzed the signaling properties of nonnetworked core complexes in live cells by following both conformational and kinase control responses to attractant stimuli and to output-biasing lesions at various locations in the receptor molecule. Contrary to the prevailing view that individual receptors are binary two-state devices, we demonstrate that conformational coupling between the ligand binding and the kinase-control receptor domains is, in fact, only moderate. In addition, we demonstrate communication between neighboring receptors through their trimer-contact domains that biases them to adopt similar signaling states. Taken together, these data suggest a view of signaling in receptor trimers that allows significant signal integration to occur within individual core complexes.

Original languageAmerican English
Pages (from-to)e2312064121
JournalProceedings of the National Academy of Sciences of the United States of America
Volume121
Issue number14
DOIs
StatePublished - 2 Apr 2024

Keywords

  • cell signaling
  • chemotaxis
  • receptor array
  • signal integration

All Science Journal Classification (ASJC) codes

  • General

Fingerprint

Dive into the research topics of 'Signal integration in chemoreceptor complexes'. Together they form a unique fingerprint.

Cite this