期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1793, 期 1, 页码 146-153出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2008.05.002
关键词
Mitochondria; Superoxide dismutase; Cytochrome c oxidase; SCO proteins; Copper trafficking
资金
- United Mitochondrial Disease Foundation [07-130]
- National Institutes of Environmental Health Sciences, NIH [ES 03817]
- Muscular Dystrophy Association [4181]
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [R01ES003817, R37ES003817] Funding Source: NIH RePORTER
Mitochondria contain two enzymes, Cu,Zn superoxide dismutase (Sod1) and cytochrome c oxidase (CcO), that require copper as a cofactor for their biological activity. The copper used for their metallation originates from a conserved, bioactive pool contained within the mitochondrial matrix, the size of which changes in response to either genetic or pharmacological manipulation of cellular copper status. Its dynamic nature implies molecular mechanisms exist that functionally couple mitochondrial copper handling with other, extramitochondrial copper trafficking pathways. The recent finding that mitochondrial proteins with established roles in CcO assembly can also effect changes in cellular copper levels by modulating copper efflux from the cell supports a mechanistic link between organellar and cellular copper metabolism. However, the proteins and molecular mechanisms that link trafficking of copper to and from the organelle with other cellular copper trafficking pathways are unknown. This review documents our current understanding of copper trafficking to. and within, the mitochondrion for metallation of CcO and Sod1; the pathways by which the two copper centers in CcO are formed; and, the interconnections between mitochondrial function and the regulation of cellular copper homeostasis. (C) 2008 Elsevier B.V. All rights reserved.
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