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Gene Review:

atad1a - ATPase family, AAA domain containing 1a

Danio rerio

Synonyms: ATPase, ATPase family AAA domain-containing protein 1-A, SO:0000704, si:zc156n3.1, zgc:101570

Jung, D.W. et al., Cibrián-Uhalte, E. et al., Senger, M.R. et al.

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Disease relevance of atad1a

The results attest to the power of screening small molecule libraries in zebrafish as a means of identifying mammalian targets and suggest the mitochondrial ATPase as a target for modulating pigmentation in both melanocytes and melanoma cells [1].

High impact information on atad1a

Na(+),K(+) ATPase is an essential ion pump involved in regulating ionic concentrations within epithelial cells [2].
Involvement of zebrafish Na+,K+ ATPase in myocardial cell junction maintenance [2].
Functional tests and pharmacological inhibition experiments demonstrate that Na(+),K(+) ATPase activity is positively regulated via an N-terminal phosphorylation site that is necessary for correct heart morphogenesis to occur, and that maintenance of ZO-1 junction belts requires ion pump activity [2].
After cadmium treatment, ATPase activity was significantly increased (53% and 48%) at 0.5 and 1 mM, respectively [3].
Oligomycin, a small molecule known to inhibit the mitochondrial ATPase, competed with PPA for its cellular target in melanocytes [1].

Biological context of atad1a

In addition, PPA was shown to alter the membrane potential of mitochondria, consistent with inhibition of the mitochondrial ATPase [1].
Identification of the F1F0 mitochondrial ATPase as a target for modulating skin pigmentation by screening a tagged triazine library in zebrafish [1].

Analytical, diagnostic and therapeutic context of atad1a

The cellular target was identified as the mitochondrial F1F0-ATP synthase (ATPase) by affinity chromatography [1].

References

Identification of the F1F0 mitochondrial ATPase as a target for modulating skin pigmentation by screening a tagged triazine library in zebrafish. Jung, D.W., Williams, D., Khersonsky, S.M., Kang, T.W., Heidary, N., Chang, Y.T., Orlow, S.J. Molecular bioSystems. (2005) [Pubmed]
Involvement of zebrafish Na+,K+ ATPase in myocardial cell junction maintenance. Cibrián-Uhalte, E., Langenbacher, A., Shu, X., Chen, J.N., Abdelilah-Seyfried, S. J. Cell Biol. (2007) [Pubmed]
In vitro effect of zinc and cadmium on acetylcholinesterase and ectonucleotidase activities in zebrafish (Danio rerio) brain. Senger, M.R., Rosemberg, D.B., Rico, E.P., de Bem Arizi, M., Dias, R.D., Bogo, M.R., Bonan, C.D. Toxicology in vitro : an international journal published in association with BIBRA. (2006) [Pubmed]

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