Opposite regulation of oligodendrocyte apoptosis by JNK3 and Pin1 after spinal cord injury

J Neurosci. 2007 Aug 1;27(31):8395-404. doi: 10.1523/JNEUROSCI.2478-07.2007.

Abstract

Although oligodendrocytes undergo apoptosis after spinal cord injury, molecular mechanisms responsible for their death have been unknown. We report that oligodendrocyte apoptosis is regulated oppositely by c-Jun N-terminal kinase 3 (JNK3) and protein interacting with the mitotic kinase, never in mitosis A I (Pin1), the actions of which converge on myeloid cell leukemia sequence-1 (Mcl-1). Activated after injury, JNK3 induces cytochrome c release by facilitating the degradation of Mcl-1, the stability of which is maintained in part by Pin1. Pin1 binds Mcl-1 at its constitutively phosphorylated site, Thr163Pro, and stabilizes it by inhibiting ubiquitination. After injury JNK3 phosphorylates Mcl-1 at Ser121Pro, facilitating the dissociation of Pin1 from Mcl-1. JNK3 thus induces Mcl-1 degradation by counteracting the protective binding of Pin1. These results are confirmed by the opposing phenotypes observed between JNK3-/- and Pin1-/- mice: oligodendrocyte apoptosis and cytochrome c release are reduced in JNK3-/- but elevated in Pin1-/- mice. This report thus unveils a mechanism by which cytochrome c release is under the opposite control of JNK3 and Pin1, regulators for which the activities are intricately coupled.

Publication types

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

MeSH terms

  • Animals
  • Apoptosis / genetics
  • Apoptosis / physiology*
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Mitogen-Activated Protein Kinase 10 / deficiency
  • Mitogen-Activated Protein Kinase 10 / genetics
  • Mitogen-Activated Protein Kinase 10 / physiology*
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Oligodendroglia / cytology
  • Oligodendroglia / enzymology*
  • Oligodendroglia / pathology
  • Peptidylprolyl Isomerase / deficiency
  • Peptidylprolyl Isomerase / genetics
  • Peptidylprolyl Isomerase / physiology*
  • Spinal Cord Injuries / enzymology*
  • Spinal Cord Injuries / genetics
  • Spinal Cord Injuries / pathology
  • Ubiquitin / antagonists & inhibitors
  • Ubiquitin / metabolism

Substances

  • NIMA-Interacting Peptidylprolyl Isomerase
  • Ubiquitin
  • Mitogen-Activated Protein Kinase 10
  • Peptidylprolyl Isomerase
  • Pin1 protein, mouse