Towards defining the substrate of orphan P5A-ATPases

Sørensen, Danny Mollerup; Holen, Henrik Waldal; Holemans, Tine; Vangheluwe, Peter; Palmgren, Michael G.

doi:10.1016/j.bbagen.2014.05.008

Cited by 43 publications

(57 citation statements)

References 134 publications

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“…P5A ATPases represent a conserved subfamily of P‐type ATPases that are present in the endoplasmic reticulum and are expected to serve an important function, as their deletion causes severe endoplasmic reticulum stress. However, their biochemical ligand has not been identified yet (Sorensen et al ). P5A pumps are easily recognizable due to specific sequence motifs in most transmembrane domains (Sorensen et al ), including a PQ.L motif in TM1 (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…However, their biochemical ligand has not been identified yet (Sorensen et al ). P5A pumps are easily recognizable due to specific sequence motifs in most transmembrane domains (Sorensen et al ), including a PQ.L motif in TM1 (Fig. S2).…”

Section: Methodsmentioning

confidence: 99%

“…Adding to this list, we identified up to three isoforms in many genomes of the protozoal supergroups Stramenopiles, Alveolata and Rhizaria (Table S1). In contrast to other P‐type ATPase subfamilies, P5A ATPases have previously been reported to typically only be present in single copies (Sorensen et al ). However, in this analysis, two copies were identified in most Stramenopiles and in the Alveolata Perkinsus marinus (Table S2).…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Evolution of P2A and P5A ATPases: ancient gene duplications and the red algal connection to green plants revisited

Palmgren

Sørensen

Hallström

et al. 2019

Physiologia Plantarum

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In a search for slowly evolving nuclear genes that may cast light on the deep evolution of plants, we carried out phylogenetic analyses of two well‐characterized subfamilies of P‐type pumps (P2A and P5A ATPases) from representative branches of the eukaryotic tree of life. Both P‐type ATPase genes were duplicated very early in eukaryotic evolution and before the divergence of the present eukaryotic supergroups. Synapomorphies identified in the sequences provide evidence that green plants and red algae are more distantly related than are green plants and eukaryotic supergroups in which secondary or tertiary plastids are common, such as several groups belonging to the clade that includes Stramenopiles, Alveolata, Rhizaria, Cryptophyta and Haptophyta (SAR). We propose that red algae branched off soon after the first photosynthesizing eukaryote had acquired a primary plastid, while in another lineage that led to SAR, the primary plastid was lost but, in some cases, regained as a secondary or tertiary plastid.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Evolution of P2A and P5A ATPases: ancient gene duplications and the red algal connection to green plants revisited

Palmgren

Sørensen

Hallström

et al. 2019

Physiologia Plantarum

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“…P5A-ATPase activity in yeast leads to pleiotropic phenotypes consistent with a failure to maintain basic ER functions, such as protein folding and processing or trafficking of secretory vesicles (Sørensen et al, 2015). Although general secretion is not severely impaired in pdr2 root meristems (Ticconi et al, 2004), disruption of AtP5A/MIA/PDR2 selectively sensitizes a subset of ER quality control responses (Ticconi et al, 2009).…”

Section: Lpr1-dependent Fe Accumulation Controls Callose Deposition Imentioning

confidence: 99%

Iron-Dependent Callose Deposition Adjusts Root Meristem Maintenance to Phosphate Availability

et al. 2015

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Plant root development is informed by numerous edaphic cues. Phosphate (Pi) availability impacts the root system architecture by adjusting meristem activity. However, the sensory mechanisms monitoring external Pi status are elusive. Two functionally interacting Arabidopsis genes, LPR1 (ferroxidase) and PDR2 (P5-type ATPase), are key players in root Pi sensing, which is modified by iron (Fe) availability. We show that the LPR1-PDR2 module facilitates, upon Pi limitation, cell-specific apoplastic Fe and callose deposition in the meristem and elongation zone of primary roots. Expression of cell-wall-targeted LPR1 determines the sites of Fe accumulation as well as callose production, which interferes with symplastic communication in the stem cell niche, as demonstrated by impaired SHORT-ROOT movement. Antagonistic interactions of Pi and Fe availability control primary root growth via meristem-specific callose formation, likely triggered by LPR1-dependent redox signaling. Our results link callose-regulated cell-to-cell signaling in root meristems to the perception of an abiotic cue.

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“…At present, the biochemical characterization of P5-ATPases is limited, and the putative transported ion has not yet been identified (16). The best characterized P5-ATPase is Spf1p.…”

Section: ؉mentioning

confidence: 99%

Inhibition of the Formation of the Spf1p Phosphoenzyme by Ca2+

Corradi

Czysezon

Mazzitelli

et al. 2016

Journal of Biological Chemistry

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P5-ATPases are important for processes associated with the endosomal-lysosomal system of eukaryotic cells. In humans, the loss of function of P5-ATPases causes neurodegeneration. In the yeast Saccharomyces cerevisiae, deletion of P5-ATPase Spf1p gives rise to endoplasmic reticulum stress. The reaction cycle of P5-ATPases is poorly characterized. Here, we showed that the formation of the Spf1p catalytic phosphoenzyme was fast in a reaction medium containing ATP, Mg 2؉ , and EGTA. . Halfmaximal phosphorylation was attained at 8 M Mg 2؉, but higher concentrations partially protected from Ca 2؉ inhibition. In conditions similar to those used for phosphorylation, Ca 2؉ had a small effect accelerating dephosphorylation and minimally affected ATPase activity, suggesting that the formation of the phosphoenzyme was not the limiting step of the ATP hydrolytic cycle.P5-ATPases comprise a group of proteins that are classified as P-ATPases based on the presence of the characteristic PATPase motifs in their primary sequence (1, 2). P5-ATPases have been found only in eukaryotes and have been recently proposed to play an essential role in the endosomal-lysosomal system (3, 4). The yeast Saccharomyces cerevisiae contains two genes coding for P5-ATPases: YEL031W, coding for Spf1p (also called Cod1p), and YOR291W, coding for Ypk9. Spf1p (sensitivity to Pichia farinosa killer toxin) was initially isolated from a mutation protecting Saccharomyces from the effect of a Pichia toxin (5). The protein was also independently identified as required for the controlled degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in the endoplasmic reticulum (ER) 3 (6). These and later studies have shown that Spf1p is located in the yeast ER and that deletion of Spf1p leads to phenotypes related to ER stress (7-9). In humans, five genes (ATP13A1-A5) code for P5-ATPases (10). Mutations in ATP13A2 have been linked to an early onset autosomal recessive form of Parkinson disease (Kufor-Rakeb syndrome) and neuronal ceroid lipofuscinosis, whereas mutations in ATP13A4 have been associated with autism spectrum disorder (11-13). P-ATPases are a large group of enzymes that couple the hydrolysis of ATP with the active transport of ions (14, 15). During the transport cycle, they transiently form a phosphoenzyme (EP) that plays a key role in the active transport mechanism. P-ATPases comprise a membrane domain (M) and a soluble portion with nucleotide binding (N), phosphorylation (P), and actuator (A) domains. These domains are involved in a kinasephosphatase reaction cycle through two major conformations, E 1 -E 2 , and the transient formation of a catalytic EP. The binding of the transported ion to the E 1 form prompts the assembly of the phosphorylation site between the ATP-bound N domain and the P domain, whereas the A domain directs the occlusion of the bound ion. When the phosphorylation reaction occurs, it initially generates the high energy E 1 ϳP intermediate and releases ADP. E 1 ϳP then changes to E 2 P, and the A domain associates with the N-...

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Towards defining the substrate of orphan P5A-ATPases

Abstract: Identification of the substrate of P5A-ATPases would throw light on an important general process in the ER that is still not fully understood. This article is part of a Special Issue entitled Structural biochemistry and biophysics of membrane proteins.

Cited by 43 publications

References 134 publications

Evolution of P2A and P5A ATPases: ancient gene duplications and the red algal connection to green plants revisited

Evolution of P2A and P5A ATPases: ancient gene duplications and the red algal connection to green plants revisited

Iron-Dependent Callose Deposition Adjusts Root Meristem Maintenance to Phosphate Availability

Inhibition of the Formation of the Spf1p Phosphoenzyme by Ca2+

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