Chapter 5. Copper-Transporting ATPases: Key Regulators of Intracellular Copper Concentration

  1. Masamitsu Futai2,
  2. Yoh Wada3 and
  3. Jack H. Kaplan4
  1. Ruslan Tsivkovskii,
  2. Tina Purnat and
  3. Svetlana Lutsenko

Published Online: 6 DEC 2005

DOI: 10.1002/3527606122.ch5

Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology

Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology

How to Cite

Tsivkovskii, R., Purnat, T. and Lutsenko, S. (2004) Copper-Transporting ATPases: Key Regulators of Intracellular Copper Concentration, in Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology (eds M. Futai, Y. Wada and J. H. Kaplan), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG. doi: 10.1002/3527606122.ch5

Editor Information

  1. 2

    Division of Biological Sciences, Nanoscience and Nanotechnology Center, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan

  2. 3

    Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan

  3. 4

    University of Illinois at Chicago, Department of Biochemistry and Molecular Genetics, 900 S. Ashland Ave., Chicago, IL 60607, USA

Author Information

  1. Department of Biochemistry and Molecular Biology, Oregon Health & Science University, 3181 S.W. Sam Jackson Park Rd., Portland, OR 97239-3098, USA

Publication History

  1. Published Online: 6 DEC 2005
  2. Published Print: 24 JUN 2004

ISBN Information

Print ISBN: 9783527306893

Online ISBN: 9783527606122

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Keywords:

  • ATPases;
  • P-type ATPases;
  • copper-transporting ATPases;
  • structural features;
  • regulators of intracellular copper concentration;
  • role of copper in cell physiology;
  • N-terminal copper-binding domain;
  • ATP-binding domain (ATP-BD);
  • transmembrane domain;
  • functional properties of copper-transporting ATPases;
  • disease mutations

Summary

This chapter contains sections titled:

  • Introduction

    • Role of Copper in Cell Physiology

    • Specific Functions of Copper-transporting ATPases in Various Organisms

      • Bacterial Copper-transporting ATPases

      • Cyanobacteria

      • Archeobacteria

      • Yeast

      • Plants

      • Caenorhabditis elegans

      • Human Copper-transporting ATPases

    • Animal Models for Menkes Disease and Wilson's Disease

  • Major Structural Features of Copper-transporting ATPases

    • Copper-transporting ATPases as Members of the P-type ATPase Family

      • Sequence Motifs in the Structure of CTAs

    • Topology and Organization of the Transmembrane Domain

    • N-terminal Copper-binding Domain

    • ATP-binding Domain (ATP-BD)

      • Homology Modeling of the ATP-binding Domain of Wilson's Disease Protein

    • A (actuator)-domain

    • C-terminal Tail

  • Functional Properties of Copper-transporting ATPases

    • Functional Complementation In Vivo

    • Biochemical Characterization of CTAs

      • Transport Characteristics of CTAs

      • ATPase Activity

      • Catalytic Phosphorylation

  • Functional Role of the N-terminal Copper-binding Domain

    • N-terminal Domain of Bacterial CTA

    • N-terminal Domain of Mammalian CTAs

  • Disease Mutations that Affect Function of MNKP and WNDP

    • Disease Mutations in the Transmembrane Domain

    • Mutations in the ATP-binding Domain

    • A-domain

    • Known Mutations in the N-terminal Domain of CTAs

  • Regulation of Copper-transporting ATPases

    • Copper Chaperones as Specific Regulators of CTAs

    • Copper-dependent Protein Trafficking of MNKP and WNDP

    • Molecular Mechanism of Copper-dependent Trafficking

    • Role of Copper Chaperone in CTA Trafficking

    • Kinase-dependent Phosphorylation of Human-copper-transporting ATPases in Response to Copper

  • Acknowledgments

  • References