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Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes

Author

Listed:
  • Subba Rao Gangi Setty

    (University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA)

  • Danièle Tenza

    (Institut Curie, Centre de Recherche, Paris F-75248, France
    Centre National de la Recherche Scientifique, UMR 144, Paris F-75248, France)

  • Elena V. Sviderskaya

    (Centre for Molecular and Metabolic Signalling, St George’s, University of London)

  • Dorothy C. Bennett

    (Centre for Molecular and Metabolic Signalling, St George’s, University of London)

  • Graça Raposo

    (Institut Curie, Centre de Recherche, Paris F-75248, France
    Centre National de la Recherche Scientifique, UMR 144, Paris F-75248, France)

  • Michael S. Marks

    (University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA)

Abstract

Metalloenzymes: getting hold of copper Copper is an important cofactor for several enzymes. In order to be loaded onto endomembrane proteins, it is translocated from the cytosol by the copper transporters ATP7A or ATP7B. It is thought that proteins acquire copper upon transit through the trans Golgi network. Setty et al. study copper transport in pigment forming cells, mouse melanocytes. The enzyme tyrosinase catalyses melanin synthesis in melanosomes and requires copper for its activity. They find that while tyrosinase acquires copper within the trans Golgi network, it is inefficient and is lost within intermediate trafficking vesicles. Tyrosinase is subsequently reloaded with copper only when it reaches melanocytes by the copper transporter ATP7A. This provides a system for cell type specific spatial control of metalloenzyme activity and prevents aberrant activation of tyrosinase during transport.

Suggested Citation

  • Subba Rao Gangi Setty & Danièle Tenza & Elena V. Sviderskaya & Dorothy C. Bennett & Graça Raposo & Michael S. Marks, 2008. "Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes," Nature, Nature, vol. 454(7208), pages 1142-1146, August.
    • Handle: RePEc:nat:nature:v:454:y:2008:i:7208:d:10.1038_nature07163
    DOI: 10.1038/nature07163
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