D-Serine made by serine racemase in Drosophila intestine plays a physiological role in sleep

Nat Commun. 2019 May 7;10(1):1986. doi: 10.1038/s41467-019-09544-9.

Abstract

Natural D-serine (D-Ser) has been detected in animals more than two decades ago, but little is known about the physiological functions of D-Ser. Here we reveal sleep regulation by endogenous D-Ser. Sleep was decreased in mutants defective in D-Ser synthesis or its receptor the N-methyl-D-aspartic receptor 1 (NMDAR1), but increased in mutants defective in D-Ser degradation. D-Ser but not L-Ser rescued the phenotype of mutants lacking serine racemase (SR), the key enzyme for D-Ser synthesis. Pharmacological and triple gene knockout experiments indicate that D-Ser functions upstream of NMDAR1. Expression of SR was detected in both the nervous system and the intestines. Strikingly, reintroduction of SR into specific intestinal epithelial cells rescued the sleep phenotype of sr mutants. Our results have established a novel physiological function for endogenous D-Ser and a surprising role for intestinal cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Behavior, Animal / physiology
  • Drosophila / physiology
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Epithelial Cells / metabolism
  • Female
  • Gene Knockout Techniques
  • Intestinal Mucosa / cytology
  • Intestinal Mucosa / metabolism
  • Male
  • Models, Animal
  • Racemases and Epimerases / genetics
  • Racemases and Epimerases / metabolism*
  • Receptors, N-Methyl-D-Aspartate / genetics
  • Receptors, N-Methyl-D-Aspartate / metabolism*
  • Serine / metabolism*
  • Sleep / physiology*
  • Stereoisomerism

Substances

  • Drosophila Proteins
  • NMDA receptor A1
  • Nmdar1 protein, Drosophila
  • Receptors, N-Methyl-D-Aspartate
  • Serine
  • Racemases and Epimerases
  • serine racemase