Dual leucine zipper kinase is required for excitotoxicity-induced neuronal degeneration

J Exp Med. 2013 Nov 18;210(12):2553-67. doi: 10.1084/jem.20122832. Epub 2013 Oct 28.

Abstract

Excessive glutamate signaling is thought to underlie neurodegeneration in multiple contexts, yet the pro-degenerative signaling pathways downstream of glutamate receptor activation are not well defined. We show that dual leucine zipper kinase (DLK) is essential for excitotoxicity-induced degeneration of neurons in vivo. In mature neurons, DLK is present in the synapse and interacts with multiple known postsynaptic density proteins including the scaffolding protein PSD-95. To examine DLK function in the adult, DLK-inducible knockout mice were generated through Tamoxifen-induced activation of Cre-ERT in mice containing a floxed DLK allele, which circumvents the neonatal lethality associated with germline deletion. DLK-inducible knockouts displayed a modest increase in basal synaptic transmission but had an attenuation of the JNK/c-Jun stress response pathway activation and significantly reduced neuronal degeneration after kainic acid-induced seizures. Together, these data demonstrate that DLK is a critical upstream regulator of JNK-mediated neurodegeneration downstream of glutamate receptor hyper-activation and represents an attractive target for the treatment of indications where excitotoxicity is a primary driver of neuronal loss.

MeSH terms

  • Animals
  • Brain / pathology
  • Brain / physiopathology
  • Disks Large Homolog 4 Protein
  • Glutamic Acid / physiology
  • Guanylate Kinases / physiology
  • Kainic Acid / toxicity
  • MAP Kinase Kinase Kinases / deficiency
  • MAP Kinase Kinase Kinases / genetics
  • MAP Kinase Kinase Kinases / physiology*
  • MAP Kinase Signaling System
  • Membrane Proteins / physiology
  • Mice
  • Mice, Knockout
  • N-Methylaspartate / physiology
  • Nerve Degeneration / genetics
  • Nerve Degeneration / pathology
  • Nerve Degeneration / physiopathology*
  • Nerve Tissue Proteins / physiology
  • Synapses / physiology

Substances

  • Disks Large Homolog 4 Protein
  • Dlg4 protein, mouse
  • Membrane Proteins
  • Nerve Tissue Proteins
  • postsynaptic density proteins
  • Glutamic Acid
  • N-Methylaspartate
  • MAP Kinase Kinase Kinases
  • mitogen-activated protein kinase kinase kinase 12
  • Guanylate Kinases
  • Kainic Acid