Autophagy induced by Alexander disease-mutant GFAP accumulation is regulated by p38/MAPK and mTOR signaling pathways

Hum Mol Genet. 2008 Jun 1;17(11):1540-55. doi: 10.1093/hmg/ddn042. Epub 2008 Feb 14.

Abstract

Glial fibrillary acidic protein (GFAP) is the principle intermediate filament (IF) protein in astrocytes. Mutations in the GFAP gene lead to Alexander disease (AxD), a rare, fatal neurological disorder characterized by the presence of abnormal astrocytes that contain GFAP protein aggregates, termed Rosenthal fibers (RFs), and the loss of myelin. All GFAP mutations cause the same histopathological defect, i.e. RFs, though little is known how the mutations affect protein accumulation as well as astrocyte function. In this study, we found that GFAP accumulation induces macroautophagy, a key clearance mechanism for prevention of aggregated proteins. This autophagic response is negatively regulated by mammalian target of rapamycin (mTOR). The activation of p38 MAPK by GFAP accumulation is in part responsible for the down-regulation of phosphorylated-mTOR and the subsequent activation of autophagy. Our study suggests that AxD mutant GFAP accumulation stimulates autophagy, in a manner regulated by p38 MAPK and mTOR signaling pathways. Autophagy, in turn, serves as a mechanism to reduce GFAP levels.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Alexander Disease / genetics*
  • Alexander Disease / metabolism*
  • Animals
  • Astrocytes / metabolism
  • Autophagy / genetics*
  • Brain / metabolism
  • Brain / ultrastructure
  • Cell Line, Tumor
  • Glial Fibrillary Acidic Protein / genetics*
  • Glial Fibrillary Acidic Protein / metabolism*
  • Humans
  • Mice
  • Mice, Mutant Strains
  • Mutation
  • Protein Kinase Inhibitors
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • RNA, Small Interfering / genetics
  • Signal Transduction
  • TOR Serine-Threonine Kinases
  • Vacuoles / metabolism
  • p38 Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • p38 Mitogen-Activated Protein Kinases / genetics
  • p38 Mitogen-Activated Protein Kinases / metabolism*

Substances

  • Glial Fibrillary Acidic Protein
  • Protein Kinase Inhibitors
  • RNA, Small Interfering
  • Protein Kinases
  • MTOR protein, human
  • mTOR protein, mouse
  • TOR Serine-Threonine Kinases
  • p38 Mitogen-Activated Protein Kinases