Relevant bibliographies by topics / P-IV ATPase

Academic literature on the topic 'P-IV ATPase'

Author: Grafiati
Published: 1 April 2023

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Journal articles on the topic "P-IV ATPase"

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Halleck, Margaret S., Robert A. Schlegel, and Patrick L. Williamson. "Reanalysis of ATP11B, a Type IV P-type ATPase." Journal of Biological Chemistry 277, no. 12 (January 14, 2002): 9736–40. http://dx.doi.org/10.1074/jbc.m200240200.

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Roland, Bartholomew P., and Todd R. Graham. "Directed evolution of a sphingomyelin flippase reveals mechanism of substrate backbone discrimination by a P4-ATPase." Proceedings of the National Academy of Sciences 113, no. 31 (July 18, 2016): E4460—E4466. http://dx.doi.org/10.1073/pnas.1525730113.

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Phospholipid flippases in the type IV P-type ATPase (P4-ATPases) family establish membrane asymmetry and play critical roles in vesicular transport, cell polarity, signal transduction, and neurologic development. All characterized P4-ATPases flip glycerophospholipids across the bilayer to the cytosolic leaflet of the membrane, but how these enzymes distinguish glycerophospholipids from sphingolipids is not known. We used a directed evolution approach to examine the molecular mechanisms through which P4-ATPases discriminate substrate backbone. A mutagenesis screen in the yeast Saccharomyces cerevisiae has identified several gain-of-function mutations in the P4-ATPase Dnf1 that facilitate the transport of a novel lipid substrate, sphingomyelin. We found that a highly conserved asparagine (N220) in the first transmembrane segment is a key enforcer of glycerophospholipid selection, and specific substitutions at this site allow transport of sphingomyelin.
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Theorin, Lisa, Kristina Faxén, Danny Mollerup Sørensen, Rebekka Migotti, Gunnar Dittmar, Jürgen Schiller, David L. Daleke, Michael Palmgren, Rosa Laura López-Marqués, and Thomas Günther Pomorski. "The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase." Biochemical Journal 476, no. 5 (March 6, 2019): 783–94. http://dx.doi.org/10.1042/bcj20180891.

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Abstract Type IV P-type ATPases (P4 ATPases) are lipid flippases that catalyze phospholipid transport from the exoplasmic to the cytoplasmic leaflet of cellular membranes, but the mechanism by which they recognize and transport phospholipids through the lipid bilayer remains unknown. In the present study, we succeeded in purifying recombinant aminophospholipid ATPase 2 (ALA2), a member of the P4 ATPase subfamily in Arabidopsis thaliana, in complex with the ALA-interacting subunit 5 (ALIS5). The ATP hydrolytic activity of the ALA2–ALIS5 complex was stimulated in a highly specific manner by phosphatidylserine. Small changes in the stereochemistry or the functional groups of the phosphatidylserine head group affected enzymatic activity, whereas alteration in the length and composition of the acyl chains only had minor effects. Likewise, the enzymatic activity of the ALA2–ALIS5 complex was stimulated by both mono- and di-acyl phosphatidylserines. Taken together, the results identify the lipid head group as the key structural element for substrate recognition by the P4 ATPase.
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Costa, Sara R., Magdalena Marek, Kristian B. Axelsen, Lisa Theorin, Thomas G. Pomorski, and Rosa L. López-Marqués. "Role of post-translational modifications at the β-subunit ectodomain in complex association with a promiscuous plant P4-ATPase." Biochemical Journal 473, no. 11 (May 27, 2016): 1605–15. http://dx.doi.org/10.1042/bcj20160207.

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P-type ATPases of subfamily IV (P4-ATPases) constitute a major group of phospholipid flippases that form heteromeric complexes with members of the Cdc50 (cell division control 50) protein family. Some P4-ATPases interact specifically with only one β-subunit isoform, whereas others are promiscuous and can interact with several isoforms. In the present study, we used a site-directed mutagenesis approach to assess the role of post-translational modifications at the plant ALIS5 β-subunit ectodomain in the functionality of the promiscuous plant P4-ATPase ALA2. We identified two N-glycosylated residues, Asn181 and Asn231. Whereas mutation of Asn231 seems to have a small effect on P4-ATPase complex formation, mutation of evolutionarily conserved Asn181 disrupts interaction between the two subunits. Of the four cysteine residues located in the ALIS5 ectodomain, mutation of Cys86 and Cys107 compromises complex association, but the mutant β-subunits still promote complex trafficking and activity to some extent. In contrast, disruption of a conserved disulfide bond between Cys158 and Cys172 has no effect on the P4-ATPase complex. Our results demonstrate that post-translational modifications in the β-subunit have different functional roles in different organisms, which may be related to the promiscuity of the P4-ATPase.
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Flamant, Stéphane, Pascale Pescher, Brigitte Lemercier, Mathieu Clément-Ziza, François Képès, Marc Fellous, Geneviève Milon, Gilles Marchal, and Claude Besmond. "Characterization of a putative type IV aminophospholipid transporter P-type ATPase." Mammalian Genome 14, no. 1 (January 1, 2003): 21–30. http://dx.doi.org/10.1007/s00335-002-3032-3.

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Hiraizumi, Masahiro, Keitaro Yamashita, Tomohiro Nishizawa, and Osamu Nureki. "Cryo-EM structures capture the transport cycle of the P4-ATPase flippase." Science 365, no. 6458 (August 15, 2019): 1149–55. http://dx.doi.org/10.1126/science.aay3353.

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In eukaryotic membranes, type IV P-type adenosine triphosphatases (P4-ATPases) mediate the translocation of phospholipids from the outer to the inner leaflet and maintain lipid asymmetry, which is critical for membrane trafficking and signaling pathways. Here, we report the cryo–electron microscopy structures of six distinct intermediates of the human ATP8A1-CDC50a heterocomplex at resolutions of 2.6 to 3.3 angstroms, elucidating the lipid translocation cycle of this P4-ATPase. ATP-dependent phosphorylation induces a large rotational movement of the actuator domain around the phosphorylation site in the phosphorylation domain, accompanied by lateral shifts of the first and second transmembrane helices, thereby allowing phosphatidylserine binding. The phospholipid head group passes through the hydrophilic cleft, while the acyl chain is exposed toward the lipid environment. These findings advance our understanding of the flippase mechanism and the disease-associated mutants of P4-ATPases.
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Xu, Zongchang, Prince Marowa, Han Liu, Haina Du, Chengsheng Zhang, and Yiqiang Li. "Genome-Wide Identification and Analysis of P-Type Plasma Membrane H+-ATPase Sub-Gene Family in Sunflower and the Role of HHA4 and HHA11 in the Development of Salt Stress Resistance." Genes 11, no. 4 (March 27, 2020): 361. http://dx.doi.org/10.3390/genes11040361.

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The P-type plasma membrane (PM) H+-ATPase plays a major role during the growth and development of a plant. It is also involved in plant resistance to a variety of biotic and abiotic factors, including salt stress. The PM H+-ATPase gene family has been well characterized in Arabidopsis and other crop plants such as rice, cucumber, and potato; however, the same cannot be said in sunflower (Helianthus annuus). In this study, a total of thirteen PM H+-ATPase genes were screened from the recently released sunflower genome database with a comprehensive genome-wide analysis. According to a systematic phylogenetic classification with a previously reported species, the sunflower PM H+-ATPase genes (HHAs) were divided into four sub-clusters (I, II, IV, and V). In addition, systematic bioinformatics analyses such as gene structure analysis, chromosome location analysis, subcellular localization predication, conserved motifs, and Cis-acting elements of promoter identification were also done. Semi-quantitative PCR analysis data of HHAs in different sunflower tissues revealed the specificity of gene spatiotemporal expression and sub-cluster grouping. Those belonging to sub-cluster I and II exhibited wide expression in almost all of the tissues studied while sub-cluster IV and V seldom showed expression. In addition, the expression of HHA4, HHA11, and HHA13 was shown to be induced by salt stress. The transgenic plants overexpressing HHA4 and HHA11 showed higher salinity tolerance compared with wild-type plants. Further analysis showed that the Na+ content of transgenic Arabidopsis plants decreased under salt stress, which indicates that PM H+ ATPase participates in the physiological process of Na+ efflux, resulting in salt resistance of the plants. This study is the first to identify and analyze the sunflower PM H+ ATPase gene family. It does not only lay foundation for future research but also demonstrates the role played by HHAs in salt stress tolerance.
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Calderón-Guzmán, David, Norma Osnaya-Brizuela, Raquel García-Alvarez, Ernestina Hernández-García, and Hugo Juárez-Olguín. "Oxidative stress induced by morphine in brain of rats fed with a protein deficient diet." Human & Experimental Toxicology 28, no. 9 (September 2009): 577–82. http://dx.doi.org/10.1177/0960327109102798.

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The objective of the study is to determine the damage by oxidative stress induced by morphine in brain of rats fed with a protein-deficient diet. Twenty-eight malnourished male Wistar rats, 30 days old, were used in the study. The animals were divided into four groups of 7 rats per group. Group I received NaCl and the groups II; III and IV intraperitoneally received 3, 6 and 12 mg/kg of morphine sulphate, respectively, in a single dose. Animals were sacrificed and the levels of glutathione (GSH), dopamine, tryptophan and 5-hydroxyindole-3-acetic acid (5-HIAA) as well as, Na+/K+ ATPase and total ATPase activity in the brain were measured. Tryptophan levels and Na+/K + ATPase activity showed non-significant changes in the experimental group. Levels of 5-HIAA decreased significantly (p = .03) in animals that received 12 mg/kg of morphine and in animals that received 3 mg/kg, levels of GSH and dopamine were found to have a significant decrease (p < .05), but a significant increase in the group that received 12 mg/kg of morphine (p < .05). Total ATPase activity increased significantly in the groups that received 3 mg/kg (p = .015) and 6 mg/kg (p = .0001) of morphine. The results show that malnutrition induces changes in cellular regulation and biochemical responses to oxidative stress caused by morphine sulphate.
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Jain, Bhawik Kumar, Bartholomew P. Roland, and Todd R. Graham. "Exofacial membrane composition and lipid metabolism regulates plasma membrane P4-ATPase substrate specificity." Journal of Biological Chemistry 295, no. 52 (October 15, 2020): 17997–8009. http://dx.doi.org/10.1074/jbc.ra120.014794.

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The plasma membrane of a cell is characterized by an asymmetric distribution of lipid species across the exofacial and cytofacial aspects of the bilayer. Regulation of membrane asymmetry is a fundamental characteristic of membrane biology and is crucial for signal transduction, vesicle transport, and cell division. The type IV family of P-ATPases, or P4-ATPases, establishes membrane asymmetry by selection and transfer of a subset of membrane lipids from the lumenal or exofacial leaflet to the cytofacial aspect of the bilayer. It is unclear how P4-ATPases sort through the spectrum of membrane lipids to identify their desired substrate(s) and how the membrane environment modulates this activity. Therefore, we tested how the yeast plasma membrane P4-ATPase, Dnf2, responds to changes in membrane composition induced by perturbation of endogenous lipid biosynthetic pathways or exogenous application of lipid. The primary substrates of Dnf2 are glucosylceramide (GlcCer) and phosphatidylcholine (PC, or their lyso-lipid derivatives), and we find that these substrates compete with each other for transport. Acutely inhibiting sphingolipid synthesis using myriocin attenuates transport of exogenously applied GlcCer without perturbing PC transport. Deletion of genes controlling later steps of glycosphingolipid production also perturb GlcCer transport to a greater extent than PC transport. In contrast, perturbation of ergosterol biosynthesis reduces PC and GlcCer transport equivalently. Surprisingly, application of lipids that are poor transport substrates differentially affects PC and GlcCer transport by Dnf2, thus altering substrate preference. Our data indicate that Dnf2 exhibits exquisite sensitivity to the membrane composition, thus providing feedback onto the function of the P4-ATPases.
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10

Zhou, X., and T. R. Graham. "Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast." Proceedings of the National Academy of Sciences 106, no. 39 (September 15, 2009): 16586–91. http://dx.doi.org/10.1073/pnas.0904293106.

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Dissertations / Theses on the topic "P-IV ATPase"

1

Liou, Angela Yen-Chun. "Characterization of members of type IV and type IIC of human P-type ATPase." Thesis, University of British Columbia, 2017. http://hdl.handle.net/2429/62488.

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P-type ATPases comprise a superfamily of proteins that play vital roles in the human body and can cause severe diseases if their functions are impaired. P₄-ATPases or type 4 of P-type ATPases are implicated in the ATP-dependent flipping of phospholipids across cell membranes. This generates and maintains transverse phospholipid asymmetry, a property important for biological processes including vesicle trafficking. ATP9A is a P₄-ATPase that remains poorly characterized despite its high expression in brain and testis. Interestingly, loss of Neo1p, the yeast ortholog of ATP9A, is lethal. The first part of this study investigates the functional properties and cellular localization of ATP9A. Human ATP9A was expressed in HEK293T cells and characterized using biochemical and cell-based approaches. ATP9A exhibited little if any phospholipid-dependent ATPase activity, but underwent hydroxylamine-sensitive phosphorylation, a characteristic feature of the P-type ATPase reaction cycle. A monoclonal antibody to ATP9A was generated for analysis of ATP9A in cells and brain tissues by western blotting and immunofluorescence microscopy. In transfected HEK293T cells ATP9A localized to perinuclear and peripheral punctate structures possibly related to the endocytic pathway. Our findings suggest that ATP9A undergoes autophosphorylation, but fails to dephosphorylate, possibly due to lack of an accessory protein or a specific substrate. Further studies on endogenous ATP9A should provide further insight into its physiological function and possible role in human disease. On the other hand, Na⁺/K⁺-ATPase (NKA) belongs to type 2C of P-type ATPases and establishes Na⁺ and K⁺ gradients across cell membranes. NKA has been shown to interact with retinoschisin (RS1), an adhesion protein essential for normal retinal structure and function. Mutations in the gene encoding RS1 cause a macular degeneration disorder called X-linked retinoschisis (XLRS). RS1 is thought to be anchored to the membranes of photoreceptor and bipolar cells through interaction with the α3 and β2 isoforms of NKA. The second part aims to characterize the RS1-NKA complex by generating monoclonal antibodies specific for the components. Indeed, immunoaffinity purification of NKAβ2 from bovine retinal membranes co-immunoprecipitated the α3 subunit and RS1. Tandem affinity purification of the native protein complexes should enhance understanding of the molecular and cellular mechanisms underlying XLRS.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate
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2

Deering, Rebecca Sue Schlegel Robert A. "Recombinant expression of type IV P-type atpases and construction of gene targeting vectors." 2009. http://etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-4231/index.html.

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3

Lyssenko, Nicholas N. "A systematic study of expression and function of Caenorhabditis elegans genes encoding P-type atpases in subfamily IV the group of putative transbilayer amphipath transporters /." 2007. http://etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-2047/index.html.

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Book chapters on the topic "P-IV ATPase"

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López-Marqués, Rosa L., Danny M. Sørensen, and Michael G. Palmgren. "Type IV (P4) and V (P5) P-ATPases in Lipid Translocation and Membrane Trafficking." In Signaling and Communication in Plants, 313–26. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-14369-4_11.

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