Changing the locks on intestinal signaling

Cell Host Microbe. 2021 Sep 8;29(9):1335-1337. doi: 10.1016/j.chom.2021.08.005.

Abstract

Endogenous peptides and structurally similar bacterial heat-stable enterotoxins (ST) bind guanylate cyclase-C (GC-C), resulting in fluid homeostasis or diarrhea, respectively. In this issue of Cell Host & Microbe, Carey et al., show how bats have evolutionarily maintained homeostatic signaling while avoiding pathogenic effects of ST.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Bacterial Toxins / metabolism*
  • Chiroptera
  • Cyclic GMP / metabolism
  • Cyclic GMP-Dependent Protein Kinase Type II / metabolism*
  • Cystic Fibrosis Transmembrane Conductance Regulator / metabolism
  • Diarrhea / microbiology
  • Diarrhea / pathology
  • Enterocytes / metabolism
  • Enterotoxigenic Escherichia coli / metabolism
  • Enterotoxigenic Escherichia coli / pathogenicity*
  • Enterotoxins / metabolism*
  • Guanylate Cyclase / genetics
  • Guanylate Cyclase / metabolism*
  • Protein Binding
  • Signal Transduction
  • Sodium-Hydrogen Exchangers / metabolism

Substances

  • Bacterial Toxins
  • Enterotoxins
  • Sodium-Hydrogen Exchangers
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Cyclic GMP-Dependent Protein Kinase Type II
  • Guanylate Cyclase
  • Cyclic GMP