INF2-mediated actin filament reorganization confers intrinsic resilience to neuronal ischemic injury

Nat Commun. 2022 Oct 13;13(1):6037. doi: 10.1038/s41467-022-33268-y.

Abstract

During early ischemic brain injury, glutamate receptor hyperactivation mediates neuronal death via osmotic cell swelling. Here we show that ischemia and excess NMDA receptor activation cause actin to rapidly and extensively reorganize within the somatodendritic compartment. Normally, F-actin is concentrated within dendritic spines. However, <5 min after bath-applied NMDA, F-actin depolymerizes within spines and polymerizes into stable filaments within the dendrite shaft and soma. A similar actinification occurs after experimental ischemia in culture, and photothrombotic stroke in mouse. Following transient NMDA incubation, actinification spontaneously reverses. Na+, Cl-, water, and Ca2+ influx, and spine F-actin depolymerization are all necessary, but not individually sufficient, for actinification, but combined they induce activation of the F-actin polymerization factor inverted formin-2 (INF2). Silencing of INF2 renders neurons vulnerable to cell death and INF2 overexpression is protective. Ischemia-induced dendritic actin reorganization is therefore an intrinsic pro-survival response that protects neurons from death induced by cell edema.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actins* / metabolism
  • Animals
  • Dendritic Spines / metabolism
  • Formins
  • Ischemia / metabolism
  • Mice
  • N-Methylaspartate* / metabolism
  • Neurons / metabolism
  • Receptors, Glutamate / metabolism
  • Receptors, N-Methyl-D-Aspartate / metabolism
  • Water / metabolism

Substances

  • Actins
  • Formins
  • INF2 protein, mouse
  • Receptors, Glutamate
  • Receptors, N-Methyl-D-Aspartate
  • Water
  • N-Methylaspartate