Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway

Nat Commun. 2016 Feb 16:7:10640. doi: 10.1038/ncomms10640.

Abstract

Brain development requires a fine-tuned copper homoeostasis. Copper deficiency or excess results in severe neuro-pathologies. We demonstrate that upon neuronal differentiation, cellular demand for copper increases, especially within the secretory pathway. Copper flow to this compartment is facilitated through transcriptional and metabolic regulation. Quantitative real-time imaging revealed a gradual change in the oxidation state of cytosolic glutathione upon neuronal differentiation. Transition from a broad range of redox states to a uniformly reducing cytosol facilitates reduction of the copper chaperone Atox1, liberating its metal-binding site. Concomitantly, expression of Atox1 and its partner, a copper transporter ATP7A, is upregulated. These events produce a higher flux of copper through the secretory pathway that balances copper in the cytosol and increases supply of the cofactor to copper-dependent enzymes, expression of which is elevated in differentiated neurons. Direct link between glutathione oxidation and copper compartmentalization allows for rapid metabolic adjustments essential for normal neuronal function.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Amidine-Lyases / metabolism*
  • Animals
  • Cation Transport Proteins / metabolism*
  • Chick Embryo
  • Copper / metabolism*
  • Copper Transport Proteins
  • Copper-Transporting ATPases
  • Cytosol
  • Electroporation
  • Glutathione / metabolism*
  • Glutathione Disulfide / metabolism
  • HEK293 Cells
  • Humans
  • Immunoblotting
  • Metallochaperones / metabolism*
  • Mixed Function Oxygenases / metabolism*
  • Molecular Chaperones
  • NADP / metabolism
  • Neurogenesis*
  • Neurons / metabolism*
  • Oxidation-Reduction*
  • Real-Time Polymerase Chain Reaction
  • Secretory Pathway*
  • Spectrophotometry, Atomic
  • Spinal Cord / cytology
  • Spinal Cord / embryology
  • Spinal Cord / metabolism

Substances

  • ATOX1 protein, human
  • Cation Transport Proteins
  • Copper Transport Proteins
  • Metallochaperones
  • Molecular Chaperones
  • NADP
  • Copper
  • Mixed Function Oxygenases
  • PAM protein, human
  • Adenosine Triphosphatases
  • Amidine-Lyases
  • ATP7A protein, human
  • Copper-Transporting ATPases
  • Glutathione
  • Glutathione Disulfide