PMID- 18522804
OWN - NLM
STAT- MEDLINE
DCOM- 20090226
LR  - 20220408
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1793
IP  - 1
DP  - 2009 Jan
TI  - "Pulling the plug" on cellular copper: the role of mitochondria in copper export.
PG  - 146-53
LID - 10.1016/j.bbamcr.2008.05.002 [doi]
AB  - 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.
FAU - Leary, Scot C
AU  - Leary SC
AD  - Montreal Neurological Institute and McGill University, Montreal, Canada H3A 2B4. 
      scot.leary@mcgill.ca
FAU - Winge, Dennis R
AU  - Winge DR
FAU - Cobine, Paul A
AU  - Cobine PA
LA  - eng
GR  - R01 ES003817/ES/NIEHS NIH HHS/United States
GR  - R37 ES003817/ES/NIEHS NIH HHS/United States
GR  - ES 03817/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20080515
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Mitochondrial Proteins)
RN  - 789U1901C5 (Copper)
RN  - EC 1.15.1.1 (Superoxide Dismutase)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Copper/*metabolism
MH  - Electron Transport Complex IV/metabolism
MH  - Humans
MH  - Mitochondria/enzymology/*metabolism
MH  - Mitochondrial Proteins/*metabolism
MH  - Models, Biological
MH  - Superoxide Dismutase/metabolism
PMC - PMC4021392
MID - NIHMS501529
EDAT- 2008/06/05 09:00
MHDA- 2009/02/27 09:00
PMCR- 2014/05/15
CRDT- 2008/06/05 09:00
PHST- 2008/03/15 00:00 [received]
PHST- 2008/05/02 00:00 [revised]
PHST- 2008/05/05 00:00 [accepted]
PHST- 2008/06/05 09:00 [pubmed]
PHST- 2009/02/27 09:00 [medline]
PHST- 2008/06/05 09:00 [entrez]
PHST- 2014/05/15 00:00 [pmc-release]
AID - S0167-4889(08)00164-X [pii]
AID - 10.1016/j.bbamcr.2008.05.002 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2009 Jan;1793(1):146-53. doi: 10.1016/j.bbamcr.2008.05.002. 
      Epub 2008 May 15.