The complete inventory of the yeast <i>Saccharomyces cerevisiae</i> P‐type transport ATPases

Catty, Patrice; d’Exaerde, Alban de Kerchove; Goffeau, André

doi:10.1016/s0014-5793(97)00446-8

Cited by 117 publications

(111 citation statements)

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“…Based on these differences, the DRS2 class has been proposed to represent a separate subfamily of P-type ATPases that transport lipids rather than cations (Tang et al, 1996). Consistent with this, phylogenetic analysis performed in this study ( Figure 5B) and by others (Catty et al, 1997) indicates that the DRS2 family of P-type ATPases diverged from a primordial P-type ATPase to perform a distinct function (Daleke and Lyles, 2000). Biochemical studies, meanwhile, have now revealed that aminophospholipid translocases, purified from erythrocytes and chromaffin granules in mammals, are phosphatidylserine-inducible, Growth of S. cerevisiae on glucose-or galactose-amended growth medium plates.…”

supporting

confidence: 88%

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 83%

“…Phylogenetic analysis showed that the PDE1 product is most closely related to P-type ATPases of the DRS2 family of putative aminophospholipid translocases, as shown in Figure 5B. It is clearly distinct from the other main classes of P-type ATPases, including the H ϩ -ATPases, Ca 2ϩ -ATPases, and Na ϩ -ATPases (all P 2 type), Cu 2ϩ -ATPases (P 1 type), and P 4 -type ATPases that have been identified so far (reviewed by Catty et al, 1997;Paulsen et al, 1998).To determine whether PDE1 was functionally related to P-type ATPases of the aminophospholipid translocase group, we subcloned a 4.6-kb intronless fragment of the PDE1 gene into pYES2 for expression under the S. cerevisiae GAL1 promoter in the atc8⌬ mutant YB853 (Ashrafi et al, 1998). The atc8⌬ mutant YB853 was generated in a screen for interactions affecting the N-myristoylation pathway in yeast, but no mutant phenotype was reported in that study (Ashrafi et al, 1998) or was known to its authors (K. Ashrafi, personal communication).…”

mentioning

confidence: 83%

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PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Balhadère

Talbot

2001

Plant Cell

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Plant infection by the rice blast fungus Magnaporthe grisea is brought about by the action of specialized infection cells called appressoria. These infection cells generate enormous turgor pressure, which is translated into an invasive force that allows a narrow penetration hypha to breach the plant cuticle. The Magnaporthe pde1 mutant was identified previously by restriction enzyme-mediated DNA integration mutagenesis and is impaired in its ability to elaborate penetration hyphae. Here we report that the pde1 mutation is the result of an insertion into the promoter of a P-type ATPase-encoding gene. Targeted gene disruption confirmed the role of PDE1 in penetration hypha development and pathogenicity but highlighted potential differences in PDE1 regulation in different Magnaporthe strains. The predicted PDE1 gene product was most similar to members of the aminophospholipid translocase group of P-type ATPases and was shown to be a functional homolog of the yeast ATPase gene ATC8 . Spatial expression studies showed that PDE1 is expressed in germinating conidia and developing appressoria. These findings implicate the action of aminophospholipid translocases in the development of penetration hyphae and the proliferation of the fungus beyond colonization of the first epidermal cell. INTRODUCTIONOne of the principal reasons why pathogenic fungi are so successful at causing plant disease is their ability to penetrate the plant cuticle directly, often using specialized infection cells called appressoria (Mendgen et al., 1996). A wide variety of fungal pathogens form appressoria, and the development of these cells involves a complex morphogenetic program that results in rapid differentiation of a highly specialized structure (Dean, 1997). The rice blast fungus Magnaporthe grisea is an important pathogen of cultivated rice and has emerged as an experimental model for the study of plant infection processes (for reviews, see Howard and Valent, 1996;Hamer and Talbot, 1998). Magnaporthe develops dome-shaped appressoria, which form at the ends of germ tubes soon after spore germination on the leaf surface. Appressoria attach strongly to the leaf and then generate enormous turgor pressure (up to 8 MPa), which is used to rupture the plant cuticle (Howard et al., 1991). The turgor inside appressoria is generated by a rapid increase in intracellular glycerol levels, which is maintained by a specialized cell wall layer containing melanin (Howard and Ferrari, 1989;de Jong et al., 1997). If melanin biosynthesis is blocked, either by chemical intervention or mutation, then Magnaporthe is unable to penetrate the plant surface and cannot cause disease (Chida and Sisler, 1987;Chumley and Valent, 1990).How such enormous cellular turgor is translated into the substantial invasive force necessary to breach the plant cell wall is not clear, but it appears to involve polarization of the cytoskeleton to the point of infection and localized cell wall modification Howard, 1990, 1992;Bechinger et al., 1999). A narrow penetration hypha forms at t...

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supporting

confidence: 88%

Section: Pde1 Encodes a P-type Atpasementioning

confidence: 83%

mentioning

confidence: 83%

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PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Balhadère

Talbot

2001

Plant Cell

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“…Samples were incubated in a 5-bromo-4-chloro-3-indolyl b-D-glucuronide (X-gluc) solution (3 mM K 3 (Fe(CN) 6 ), 3 M K 4 (Fe(CN) 6 ), 0.2% Triton-X-100, 50 mM KH 2 PO 4 /K 2 HPO 4 pH 7.2, 2 mM X-gluc) at 37°C in the dark for the times specified. After incubation, samples were cleared in 96% ethanol.…”

Section: Yeast Microsomal Membrane Preparation and Immunodetectionmentioning

confidence: 99%

“…The P4-ATPases present in Saccharomyces cerevisiae are well characterized, and are involved in phospholipid translocation and vesiculation. In total, S. cerevisiae harbours five members of this family 6 , namely Neo1p (Neomycin resistant 1) 7 , Drs2p (Deficient for Ribosomal Subunit 2) 8 , Dnf1p (Drs2p/Neo1p family), Dnf2p and Dnf3p 9 . Neo1p is the only essential member 7 of the family while the four remaining members can be knocked out in all combinations, except for all four at once, without leading to lethality 9 .…”

mentioning

confidence: 99%

A phospholipid uptake system in the model plant Arabidopsis thaliana

et al. 2015

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Plants use solar energy to produce lipids directly from inorganic elements and are not thought to require molecular systems for lipid uptake from the environment. Here we show that Arabidopsis thaliana Aminophospholipid ATPase10 (ALA10) is a P4-type ATPase flippase that internalizes exogenous phospholipids across the plasma membrane, after which they are rapidly metabolized. ALA10 expression and phospholipid uptake are high in the epidermal cells of the root tip and in guard cells, the latter of which regulate the size of stomatal apertures to modulate gas exchange. ALA10-knockout mutants exhibit reduced phospholipid uptake at the root tips and guard cells and are affected in growth and transpiration. The presence of a phospholipid uptake system in plants is surprising. Our results suggest that one possible physiological role of this system is to internalize lysophosphatidylcholine, a signalling lipid involved in root development and stomatal control.

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Substrate Specificity of the Aminophospholipid Flippase

Cook¹,

Daleke²

2011

Transmembrane Dynamics of Lipids

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The complete inventory of the yeast Saccharomyces cerevisiae P‐type transport ATPases

Cited by 117 publications

References 56 publications

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

A phospholipid uptake system in the model plant Arabidopsis thaliana

Substrate Specificity of the Aminophospholipid Flippase

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