Copper chaperone Atox1 plays role in breast cancer cell migration
نویسندگان
چکیده
منابع مشابه
Conserved residues modulate copper release in human copper chaperone Atox1.
It is unclear how the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson and Menkes disease proteins in the cytoplasm. To begin to address this problem, we have characterized Cu(I) release from wild-type Atox1 and two point mutants (Met(10)Ala and Lys(60)Ala). The dynamics of Cu(I) displacement from holo-Atox1 were measured by using the Cu(I) chelator bicinchonic a...
متن کاملThe Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution
Human antioxidant protein 1 (Atox1) is a small cytosolic protein with an essential role in copper homeostasis. Atox1 functions as a copper carrier facilitating copper transfer to the secretory pathway. This process is required for activation of copper dependent enzymes involved in neurotransmitter biosynthesis, iron efflux, neovascularization, wound healing, and regulation of blood pressure. Re...
متن کاملThe metallochaperone Atox1 plays a critical role in perinatal copper homeostasis.
Copper plays a fundamental role in the biochemistry of all aerobic organisms. The delivery of this metal to specific intracellular targets is mediated by metallochaperones. To elucidate the role of the metallochaperone Atox1, we analyzed mice with a disruption of the Atox1 locus. Atox1(-/-) mice failed to thrive immediately after birth, with 45% of pups dying before weaning. Surviving animals e...
متن کاملCopper accumulation and compartmentalization in mouse fibroblast lacking metallothionein and copper chaperone, Atox1.
Copper (Cu) is the active center of some enzymes because of its redox-active property, although that property could have harmful effects. Because of this, cells have strict regulation/detoxification systems for this metal. In this study, multi-disciplinary approaches, such as speciation and elemental imaging of Cu, were applied to reveal the detoxification mechanisms for Cu in cells bearing a d...
متن کاملConserved residue modulates copper-binding properties through structural dynamics in human copper chaperone Atox1.
The human copper chaperone Atox1 plays a central role in the transport of copper in cells. It has been reported that the conserved residue Lys60 contributes to the heterocomplex stability of Atox1 with its target protein ATPase, and that the K60A mutation could diminish the copper transfer. In this work, we carried out the structure determination and dynamic analysis of Atox1 with the K60A muta...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2017
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2016.12.148