Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer's disease

Science. 2021 Jan 15;371(6526):eaaw0843. doi: 10.1126/science.aaw0843. Epub 2020 Dec 3.

Abstract

Here we describe mechanistically distinct enzymes (a kinase, a guanosine triphosphatase, and a ubiquitin protein hydrolase) that function in disparate biochemical pathways and can also act in concert to mediate a series of redox reactions. Each enzyme manifests a second, noncanonical function-transnitrosylation-that triggers a pathological biochemical cascade in mouse models and in humans with Alzheimer's disease (AD). The resulting series of transnitrosylation reactions contributes to synapse loss, the major pathological correlate to cognitive decline in AD. We conclude that enzymes with distinct primary reaction mechanisms can form a completely separate network for aberrant transnitrosylation. This network operates in the postreproductive period, so natural selection against such abnormal activity may be decreased.

Publication types

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

MeSH terms

  • Alzheimer Disease / enzymology*
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / metabolism
  • Animals
  • Cyclin-Dependent Kinase 5 / metabolism*
  • Cysteine / genetics
  • Cysteine / metabolism
  • Disease Models, Animal
  • Dynamins / metabolism*
  • HEK293 Cells
  • Humans
  • Mice
  • Mice, Transgenic
  • Mutation
  • Nitric Oxide / metabolism*
  • Nitric Oxide Synthase / metabolism*
  • Nitroarginine / pharmacology
  • Oxidation-Reduction
  • Protein Processing, Post-Translational / drug effects
  • Synapses / enzymology*
  • Synapses / pathology
  • Ubiquitin Thiolesterase / genetics
  • Ubiquitin Thiolesterase / metabolism

Substances

  • Amyloid beta-Peptides
  • UCHL1 protein, human
  • Nitroarginine
  • Nitric Oxide
  • Nitric Oxide Synthase
  • Cyclin-Dependent Kinase 5
  • CDK5 protein, human
  • Ubiquitin Thiolesterase
  • DNM1L protein, human
  • Dynamins
  • Cysteine