ArticleThe Journal of biological chemistry2012
Ca2+ induces spontaneous dephosphorylation of a novel P5A-type ATPase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Tail-anchored protein C-terminal domains stimulate ATP hydrolysis by the P5A-ATPase Spf1p.The Journal of biological chemistry · 2026Article
- Lipid flippases as key players in plant adaptation to their environment.Nature plants · 2021Review
- Dynamic membranes: the multiple roles of P4 and P5 ATPases.Plant physiology · 2021Article
- A computational framework for a Lyapunov-enabled analysis of biochemical reaction networks.PLoS computational biology · 2020Article
- Article
- The P5A ATPase Spf1p is stimulated by phosphatidylinositol 4-phosphate and influences cellular sterol homeostasis.Molecular biology of the cell · 2019Article
- The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase.The Biochemical journal · 2019Article
- Article
- Loss-of-function mutations in the ATP13A2/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78).Brain : a journal of neurology · 2017Article
- Inhibition of the Formation of the Spf1p Phosphoenzyme by Ca2.The Journal of biological chemistry · 2016Article
- A lipid switch unlocks Parkinson's disease-associated ATP13A2.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Cellular function and pathological role of ATP13A2 and related P-type transport ATPases in Parkinson's disease and other neurological disorders.Frontiers in molecular neuroscience · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P5 ATPases constitute the least studied group of P-type ATPases, an essential family of ion pumps in all kingdoms of life. Although P5 ATPases are present in every eukaryotic genome analyzed so far, they have remained orphan pumps, and their biochemical function is obscure. We show that a P5A ATPase from barley, HvP5A1, locates to the endoplasmic reticulum and is able to rescue knock-out mutants of P5A genes in both Arabidopsis thaliana and Saccharomyces cerevisiae. HvP5A1 spontaneously forms a phosphorylated reaction cycle intermediate at the catalytic residue Asp-488, whereas, among all plant nutrients tested, only Ca(2+) triggers dephosphorylation. Remarkably, Ca(2+)-induced dephosphorylation occurs at high apparent [Ca(2+)] (K(i) = 0.25 mM) and is independent of the phosphatase motif of the pump and the putative binding site for transported ligands located in M4. Taken together, our results rule out that Ca(2+) is a transported substrate but indicate the presence of a cytosolic low affinity Ca(2+)-binding site, which is conserved among P-type pumps and could be involved in pump regulation. Our work constitutes the first characterization of a P5 ATPase phosphoenzyme and points to Ca(2+) as a modifier of its function.
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