» Articles » PMID: 18534184

Cellular Multitasking: the Dual Role of Human Cu-ATPases in Cofactor Delivery and Intracellular Copper Balance

Overview
Publisher Elsevier
Specialties Biochemistry
Biophysics
Date 2008 Jun 7
PMID 18534184
Citations 66
Authors
Affiliations
Soon will be listed here.
Abstract

The human copper-transporting ATPases (Cu-ATPases) are essential for dietary copper uptake, normal development and function of the CNS, and regulation of copper homeostasis in the body. In a cell, Cu-ATPases maintain the intracellular concentration of copper by transporting copper into intracellular exocytic vesicles. In addition, these P-type ATPases mediate delivery of copper to copper-dependent enzymes in the secretory pathway and in specialized cell compartments such as secretory granules or melanosomes. The multiple functions of human Cu-ATPase necessitate complex regulation of these transporters that is mediated through the presence of regulatory domains in their structure, posttranslational modification and intracellular trafficking, as well as interactions with the copper chaperone Atox1 and other regulatory molecules. In this review, we summarize the current information on the function and regulatory mechanisms acting on human Cu-ATPases ATP7A and ATP7B. Brief comparison with the Cu-ATPase orthologs from other species is included.

Citing Articles

Review to Elucidate the Correlation between Cuproptosis-Related Genes and Immune Infiltration for Enhancing the Detection and Treatment of Cervical Cancer.

Pandey P, Ramniwas S, Pandey S, Lakhanpal S, Padmapriya G, Mishra S Int J Mol Sci. 2024; 25(19).

PMID: 39408933 PMC: 11477161. DOI: 10.3390/ijms251910604.


Pyrene-acylhydrazone-based Turn-on Fluorescent Probe for Highly Sensitive Detection Cu and Application in Bioimaging.

Liu L, Zhang H, Gao Y, Zhu H, Yang H, Zhang R J Fluoresc. 2023; 34(6):2593-2600.

PMID: 37851213 DOI: 10.1007/s10895-023-03465-z.


Abnormalities in Copper Status Associated with an Elevated Risk of Parkinson's Phenotype Development.

Karpenko M, Muruzheva Z, Ilyechova E, Babich P, Puchkova L Antioxidants (Basel). 2023; 12(9).

PMID: 37759957 PMC: 10525645. DOI: 10.3390/antiox12091654.


α-lipoic acid ameliorates consequences of copper overload by up-regulating selenoproteins and decreasing redox misbalance.

Kabin E, Dong Y, Roy S, Smirnova J, Smith J, Ralle M Proc Natl Acad Sci U S A. 2023; 120(40):e2305961120.

PMID: 37751556 PMC: 10556618. DOI: 10.1073/pnas.2305961120.


Wilson disease-causing mutations in the carboxyl terminus of ATP7B regulates its localization and Golgi exit selectively in the unpolarized cells.

Chakraborty K, Das S, Pal A, Maji S, Rai B, Gupta A Metallomics. 2023; 15(9).

PMID: 37660282 PMC: 10506129. DOI: 10.1093/mtomcs/mfad051.


References
1.
Das S, Ray K . Wilson's disease: an update. Nat Clin Pract Neurol. 2006; 2(9):482-93. DOI: 10.1038/ncpneuro0291. View

2.
Tottey S, Rich P, Rondet S, Robinson N . Two Menkes-type atpases supply copper for photosynthesis in Synechocystis PCC 6803. J Biol Chem. 2001; 276(23):19999-20004. DOI: 10.1074/jbc.M011243200. View

3.
Hirano K, Ogihara T, Ogihara H, Hiroi M, Hasegawa M, Tamai H . Identification of apo- and holo-forms of ceruloplasmin in patients with Wilson's disease using native polyacrylamide gel electrophoresis. Clin Biochem. 2004; 38(1):9-12. DOI: 10.1016/j.clinbiochem.2004.09.008. View

4.
Safaei R, Otani S, Larson B, Rasmussen M, Howell S . Transport of cisplatin by the copper efflux transporter ATP7B. Mol Pharmacol. 2007; 73(2):461-8. DOI: 10.1124/mol.107.040980. View

5.
Michalczyk A, Bastow E, Greenough M, Camakaris J, Freestone D, Taylor P . ATP7B expression in human breast epithelial cells is mediated by lactational hormones. J Histochem Cytochem. 2008; 56(4):389-99. PMC: 2326107. DOI: 10.1369/jhc.7A7300.2008. View