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Since full occupancy of the tetrahedral cavity is a common feature of all Atox1 dimeric structures obtained with other metal ions (Cu(+), Cd(2 (show CD2 Proteins)+), and Hg(2+)), we propose that in the case of platinum, where the occupancy is only 0.4, the remaining cavities are occupied by Cu(+) ions
Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 interact with nucleotide-binding domain of ATP7B (show ATP7B Proteins), thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 activate ATP7B (show ATP7B Proteins) ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B (show ATP7B Proteins) = Cu-binding P type ATPase (show ATP7A Proteins) ATP7B (show ATP7B Proteins))
It show that copper(I) and glutathione form large polymers with a molecular mass of approximately 8 kDa, which can transfer copper to Atox1.
Highlighted in this review are unique redox properties of Atox1 and other copper chaperones. Also, summarized are the redox nodes in the cytosol which potentially play dominant roles in the redox regulation of copper chaperones
The structural flexibility of the human copper chaperone Atox1 has been reported based on insights from combined pulsed EPR (show EREG Proteins) studies and computations.
Cu chaperone Atox1 has a role in breast cancer cell migration
Multiple genetic models identified genetic associations with systolic blood pressure and ATOX1.
In addition to Atox1, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (show SOD1 Proteins) (i.e. CCS (show CCS Proteins)) and cytochrome c (show CYCS Proteins) oxidase in mitochondria (i.e. Cox17 (show COX17 Proteins)). [review]
results suggest the possibility of a therapy with copper-chelating or ionophore drugs in subtypes of tumors showing specific alterations in ATOX1 expression
C-Terminus of Human Copper Importer Ctr1 (show SLC31A1 Proteins) Acts as a Binding Site and Transfers Copper to Atox1
ATOX1 appeared ubiquitously expressed throughout the cells until compaction; in subsequent embryo stages, ATOX1 relocalized to cytoplasmic perinuclear domains in the inner cell mass. Silencing of Oct4 (show POU5F1 Proteins) did not affect Atox1 expression, but silencing of Atox1 at the 2-cell stage strongly diminished Oct4 (show POU5F1 Proteins) expression in 16-cell embryos.
Cu chaperone function of Atox1 mediated through Cu transporter ATP7A (show ATP7A Proteins) is required for VEGF (show VEGFA Proteins)-induced angiogenesis via activation of Cu enzyme lysyl oxidase (show LOX Proteins).
Atox1 is involved in neointimal formation after vascular injury through promoting vascular smooth muscle cell migration and inflammatory cell recruitment in injured vessels
Atox1 functions to prevent Ang II (show AGT Proteins)-induced endothelial dysfunction and hypercontraction in resistant vessels, as well as hypertension.
the importance of Atox1, not only as a metallochaperone for delivering Cu to cuproenzymes, but also as a key player in maintaining the proper distribution and organization of Cu at the cellular level
ATOX1 is a cytoplasmic copper chaperone that interacts with the copper-binding domain of the membrane copper transporters ATP7A (show ATP7A Proteins) and ATP7B (show ATP7B Proteins)
Atox1 has a role in establishing the threshold for copper-dependent movement of the copper-transporting ATPases within the secretory compartment
Atox1 functions not only as a copper chaperone for SOD3 (show SOD3 Proteins) but also as a positive regulator for SOD3 (show SOD3 Proteins) transcription and may have an important role in modulating oxidative stress in the cardiovascular system.
Atox1 functions as a novel transcription factor that, when activated by copper, undergoes nuclear translocation, DNA binding, and transactivation, thereby contributing to cell proliferation.
both the copper chaperone and the transcription factor functions are required for the activity of antioxidant enzyme, superoxide dismutase (SOD3 (show SOD3 Proteins))
results clearly reveal a distorted copper homeostasis in Atox1-deficient Drosophila
This gene encodes a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. This protein also functions as an antioxidant against superoxide and hydrogen peroxide, and therefore, may play a significant role in cancer carcinogenesis. Because of its cytogenetic location, this gene represents a candidate gene for 5q-syndrome.
ATX1 antioxidant protein 1 homolog
, copper transport protein ATOX1
, metal transport protein ATX1
, copper chaperone
, Copper transport protein ATOX1
, ATX1 (antioxidant protein 1) homolog 1
, ATX1 homolog protein Rah1
, copper chaperone SAH
, ATX1 antioxidant protein 1 homolog (yeast)
, antioxidant protein 1 homolog