Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP

Mol Cell Biol. 2008 Jan;28(1):293-301. doi: 10.1128/MCB.00473-07. Epub 2007 Oct 22.

Abstract

Binding immunoglobulin protein (BiP) is an endoplasmic reticulum (ER) molecular chaperone that is central to ER function. We examined knock-in mice expressing a mutant BiP in order to elucidate physiological processes that are sensitive to BiP functions during development and adulthood. The mutant BiP lacked the retrieval sequence that normally functions to return BiP to the ER from the secretory pathway. This allowed us to examine the effects of a defect in ER function without completely eliminating BiP function. The homozygous mutant BiP neonates died after birth due to respiratory failure. Besides that, the mutant BiP mice displayed disordered layer formation in the cerebral cortex and cerebellum, a neurological phenotype of reeler mutant-like malformation. Consistent with the phenotype, Cajal-Retzius (CR) cells did not secrete reelin, and the expression of reelin was markedly reduced posttranscriptionally. Furthermore, the reduction in the size of the whole brain and the apparent scattering of CR cells throughout the cortex, which were distinct from the reeler phenotype, were also seen. These findings suggest that the maturation and secretion of reelin in CR cells and other factors related to neural migration may be sensitive to aberrant ER quality control, which may cause various neurological disorders.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain Diseases / congenital
  • Brain Diseases / genetics
  • Brain Diseases / metabolism*
  • Brain Diseases / pathology*
  • Cell Adhesion Molecules, Neuronal / genetics
  • Cell Adhesion Molecules, Neuronal / metabolism
  • Cerebral Cortex / abnormalities*
  • Cerebral Cortex / pathology
  • Down-Regulation
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum Chaperone BiP
  • Extracellular Matrix Proteins / genetics
  • Extracellular Matrix Proteins / metabolism
  • Gene Expression Regulation, Developmental*
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism*
  • Mice
  • Mice, Transgenic
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism*
  • Mutation / genetics
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Protein Folding
  • RNA, Messenger / genetics
  • Reelin Protein
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism

Substances

  • Cell Adhesion Molecules, Neuronal
  • Endoplasmic Reticulum Chaperone BiP
  • Extracellular Matrix Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Mutant Proteins
  • Nerve Tissue Proteins
  • RNA, Messenger
  • Reelin Protein
  • Reln protein, mouse
  • Serine Endopeptidases