Gene Review:
ATX2 - Mn(2+) transporter ATX2
Saccharomyces cerevisiae S288c
Synonyms:
Metal homeostasis factor ATX2, YOR079C, YOR29-30
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Disease relevance of ATX2
- Oxygen toxicity in Saccharomyces cerevisiae lacking the copper/zinc superoxide dismutase (SOD1) can be suppressed by overexpression of the S. cerevisiae ATX2 gene [1].
High impact information on ATX2
- The effect of ATX2 overexpression on manganese accumulation and oxygen resistance is similar to what we have previously reported for mutations in PMR1, which encodes a manganese-trafficking protein that also resides in a vesicular compartment [1].
- Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles [1].
- Multiple copies of ATX2 were found to reverse the aerobic auxotrophies of sod1(delta) mutants for lysine and methionine and also to enhance the resistance of these yeast strains to paraquat and atmospheric levels of oxygen [1].
- Third, ATX2 was incapable of suppressing oxidative damage in cells depleted of manganese ions or lacking the plasma membrane transporter for manganese [1].
- With indirect immunofluorescence microscopy, Atx2p exhibited a punctate pattern of staining typical of the Golgi apparatus, and upon subcellular fractionation, Atx2p colocalized with a biochemical marker for the yeast Golgi apparatus [1].
Biological context of ATX2
- Our studies are consistent with a model in which Atx2p and Pmr1p work in opposite directions to control manganese homeostasis [1].
Anatomical context of ATX2
- Our studies indicate that Atx2p localizes to the membrane of a vesicular compartment in yeast cells reminiscent of the Golgi apparatus [1].
Associations of ATX2 with chemical compounds
References
- Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles. Lin, S.J., Culotta, V.C. Mol. Cell. Biol. (1996) [Pubmed]
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