ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells

Ilia Voskoboinik; Hilary Brooks; Suzanne Smith; Peiyan Shen; James Camakaris

doi:10.1016/s0014-5793(98)01059-x

ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells

Ilia Voskoboinik, Hilary Brooks, Suzanne Smith, Peiyan Shen, James Camakaris

Research output: Contribution to journal › Article › peer-review

62 Citations (Scopus)

Abstract

The Menkes (MNK) protein is a vital component of copper homeostasis in mammalian cells. In this paper we provide the first biochemical evidence that the MNK protein functions as a copper-translocating P-type ATPase in mammalian cells. The enzyme activity in membrane vesicles prepared from Chinese hamster ovary cells overexpressing MNK was ATP-dependent, correlated with the amount of MNK and followed Michaelis-Menten kinetics with respect to copper. The copper transport was observed only under reducing conditions suggesting MNK transports Cu(I). This study opens the way to detailed structure-function studies and assessment of functional MNK derived from patients with Menkes disease. Copyright (C) 1998 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	178-182
Number of pages	5
Journal	FEBS Letters
Volume	435
Issue number	2-3
DOIs	https://doi.org/10.1016/s0014-5793(98)01059-x https://doi.org/10.1016/S0014-5793(98)01059-X
Publication status	Published or Issued - 18 Sep 1998
Externally published	Yes

Keywords

Copper
Copper transport
Menkes disease
P-type ATPase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells",

abstract = "The Menkes (MNK) protein is a vital component of copper homeostasis in mammalian cells. In this paper we provide the first biochemical evidence that the MNK protein functions as a copper-translocating P-type ATPase in mammalian cells. The enzyme activity in membrane vesicles prepared from Chinese hamster ovary cells overexpressing MNK was ATP-dependent, correlated with the amount of MNK and followed Michaelis-Menten kinetics with respect to copper. The copper transport was observed only under reducing conditions suggesting MNK transports Cu(I). This study opens the way to detailed structure-function studies and assessment of functional MNK derived from patients with Menkes disease. Copyright (C) 1998 Federation of European Biochemical Societies.",

keywords = "Copper, Copper transport, Menkes disease, P-type ATPase",

author = "Ilia Voskoboinik and Hilary Brooks and Suzanne Smith and Peiyan Shen and James Camakaris",

note = "Funding Information: This work was supported by the National Health and Medical Research Council, Australian Institute of Nuclear Science and Engineering, and Australian Research Council. Dr P. Shen was supported by a J.N. Peters Bequest. The authors thank Dr Z. Xiao for the ESR analysis and Dr J. Mercer and Dr L. Kelly for valuable discussions and comments on the manuscript.",

year = "1998",

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doi = "10.1016/s0014-5793(98)01059-x",

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pages = "178--182",

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T1 - ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells

AU - Voskoboinik, Ilia

AU - Brooks, Hilary

AU - Smith, Suzanne

AU - Shen, Peiyan

AU - Camakaris, James

N1 - Funding Information: This work was supported by the National Health and Medical Research Council, Australian Institute of Nuclear Science and Engineering, and Australian Research Council. Dr P. Shen was supported by a J.N. Peters Bequest. The authors thank Dr Z. Xiao for the ESR analysis and Dr J. Mercer and Dr L. Kelly for valuable discussions and comments on the manuscript.

PY - 1998/9/18

Y1 - 1998/9/18

N2 - The Menkes (MNK) protein is a vital component of copper homeostasis in mammalian cells. In this paper we provide the first biochemical evidence that the MNK protein functions as a copper-translocating P-type ATPase in mammalian cells. The enzyme activity in membrane vesicles prepared from Chinese hamster ovary cells overexpressing MNK was ATP-dependent, correlated with the amount of MNK and followed Michaelis-Menten kinetics with respect to copper. The copper transport was observed only under reducing conditions suggesting MNK transports Cu(I). This study opens the way to detailed structure-function studies and assessment of functional MNK derived from patients with Menkes disease. Copyright (C) 1998 Federation of European Biochemical Societies.

AB - The Menkes (MNK) protein is a vital component of copper homeostasis in mammalian cells. In this paper we provide the first biochemical evidence that the MNK protein functions as a copper-translocating P-type ATPase in mammalian cells. The enzyme activity in membrane vesicles prepared from Chinese hamster ovary cells overexpressing MNK was ATP-dependent, correlated with the amount of MNK and followed Michaelis-Menten kinetics with respect to copper. The copper transport was observed only under reducing conditions suggesting MNK transports Cu(I). This study opens the way to detailed structure-function studies and assessment of functional MNK derived from patients with Menkes disease. Copyright (C) 1998 Federation of European Biochemical Societies.

KW - Copper

KW - Copper transport

KW - Menkes disease

KW - P-type ATPase

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U2 - 10.1016/s0014-5793(98)01059-x

DO - 10.1016/s0014-5793(98)01059-x

M3 - Article

C2 - 9762903

VL - 435

SP - 178

EP - 182

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2-3

ER -

ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells

Abstract

Keywords

ASJC Scopus subject areas

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