Atx1-like chaperones and their cognate P-type ATPases: Copper-binding and transfer

Chloe Singleton; Nick E. Le Brun

doi:10.1007/s10534-006-9068-1

Atx1-like chaperones and their cognate P-type ATPases: Copper-binding and transfer

Chloe Singleton
, Nick E. Le Brun

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

49 Citations (Scopus)

Abstract

Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P_1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.

Original language	English
Pages (from-to)	275-289
Number of pages	15
Journal	BioMetals
Volume	20
Issue number	3-4
DOIs	https://doi.org/10.1007/s10534-006-9068-1
Publication status	Published - Jun 2007

Keywords

Atx1
Chaperone
Copper trafficking
Copper transfer
CopZ
P-type ATPase

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10.1007/s10534-006-9068-1

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abstract = "Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.",

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AB - Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.

KW - Atx1

KW - Chaperone

KW - Copper trafficking

KW - Copper transfer

KW - CopZ

KW - P-type ATPase

UR - https://www.scopus.com/pages/publications/34248661549

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JF - BioMetals

IS - 3-4

ER -

Atx1-like chaperones and their cognate P-type ATPases: Copper-binding and transfer

Abstract

Keywords

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