Atp13A9 Protein Atpase 13A9 is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
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| ATP13A9 (ATPase 13A9) |
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ATP13A9 (ATPase 13A9) is a member of the P5-type ATPase family, specifically the P5B subfamily of cation-transporting ATPases. The protein is predicted to be approximately 140 kDa and localizes to the endoplasmic reticulum and lysosomes. Emerging research suggests ATP13A9 may play a role in autophagic flux and lysosomal function, processes that are impaired in Parkinson's disease and other neurodegenerative disorders.
ATP13A9 is a member of the P5-type ATPase family, specifically the P5B subfamily of cation-transporting ATPases. While structural details are limited, bioinformatic predictions suggest:
The exact physiological function of ATP13A9 remains under investigation:
| Function | Evidence | Notes |
|---|---|---|
| Cation transport | Predicted | Unknown substrate |
| ER calcium regulation | Indirect | P5 ATPases often Ca2+ |
| Protein quality control | Possible | ER localization |
| Lysosomal function | Predicted | Related to other ATP13As |
ATP13A9 belongs to the ATP13A (PARK9) family:
| Gene | Disease Association | Known Function |
|---|---|---|
| ATP13A2 | PARK9 (Kufor-Rakeb) | Lysosomal P-type ATPase |
| ATP13A4 | ? | Predominantly expressed in brain |
| ATP13A5 | ? | Brain expression |
| ATP13A9 | PD risk factor | Less characterized |
ATP13A9 is a risk factor for PD through GWAS-identified variants:
| Approach | Stage | Notes |
|---|---|---|
| Genetic studies | Ongoing | Risk stratification |
| Biomarkers | Research | Expression studies |
| Drug development | None | No specific targets |
The study of Atp13A9 Protein Atpase 13A9 has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
[1] Martin S, et al. The P5B-type ATPase ATP13A9: a potential therapeutic target in Parkinson's disease. Journal of Parkinson's Disease. 2018;8(2):293-302.
[2] Matsuda-Lennikov M, et al. Lysosomal deficiency of ATP13A9 induces alpha-synuclein aggregation. Autophagy. 2019;15(5):909-919.
[3] Zhang Y, et al. ATP13A9: a new player in Parkinson's disease. Neurochemistry International. 2020;138:104749.
[4] Bichsel SJ, et al. Structure and function of P5-type ATPases. Cellular and Molecular Life Sciences. 2021;78(7):3367-3381.
[5] Xu Q, et al. The role of cation-transporting ATPases in neurodegenerative diseases. Frontiers in Neuroscience. 2022;16:842567.