A P-type ATPase required for rice blast disease and induction of host resistance

Gilbert, Martin; Thornton, Christopher R.; Wakley, Gavin E.; Talbot, Nicholas J.

doi:10.1038/nature04567

Cited by 98 publications

(93 citation statements)

References 25 publications

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“…In A. thaliana, ALA3 is essential for the formation of post-Golgi vesicles in actively secreting cells at the plant root tip (Poulsen et al, 2008). Taken together with the trafficking defects found in P 4 -ATPase mutant strains of fungal and plant pathogens (Gilbert et al, 2006;Hu and Kronstad, 2010), these data support a fundamental role of P 4 -ATPases in vesicle formation at late secretory and endosomal organelles.…”

Section: Flippases Participate In Key Biological Processes Vesicular supporting

confidence: 58%

Inner workings and biological impact of phospholipid flippases

Panatala

Hennrich

Holthuis

2015

Journal of Cell Science

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The plasma membrane, trans-Golgi network and endosomal system of eukaryotic cells are populated with flippases that hydrolyze ATP to help establish asymmetric phospholipid distributions across the bilayer. Upholding phospholipid asymmetry is vital to a host of cellular processes, including membrane homeostasis, vesicle biogenesis, cell signaling, morphogenesis and migration. Consequently, defining the identity of flippases and their biological impact has been the subject of intense investigations. Recent work has revealed a remarkable degree of kinship between flippases and cation pumps. In this Commentary, we review emerging insights into how flippases work, how their activity is controlled according to cellular demands, and how disrupting flippase activity causes system failure of membrane function, culminating in membrane trafficking defects, aberrant signaling and disease.

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Section: Flippases Participate In Key Biological Processes Vesicular supporting

confidence: 58%

Inner workings and biological impact of phospholipid flippases

Panatala

Hennrich

Holthuis

2015

Journal of Cell Science

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“…At least initially, AVR-Pita1 appears to be secreted into BICs using the normal fungal ER-mediated secretion machinery because mutation in the ER chaperone LHS1 with a role in secretion severely impairs its BIC accumulation and its function in triggering Pita-mediated HR (Yi et al, 2009). Another study suggested that M. oryzae uses different secretion mechanisms in planta because the APT2 gene, which encodes a Golgi-localized P-type ATPase, appears to only be involved in secretion of the tested AVR effector and a subset of extracellular enzymes (Gilbert et al, 2006). N-terminal signal sequences, though seemingly highly conserved in function, can specify diverse targeting pathways, determine efficiency of translocation, and even have postcleavage functions (Hegde and Bernstein, 2006;Cross et al, 2009).…”

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

et al. 2010

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Knowledge remains limited about how fungal pathogens that colonize living plant cells translocate effector proteins inside host cells to regulate cellular processes and neutralize defense responses. To cause the globally important rice blast disease, specialized invasive hyphae (IH) invade successive living rice (Oryza sativa) cells while enclosed in host-derived extrainvasive hyphal membrane. Using live-cell imaging, we identified a highly localized structure, the biotrophic interfacial complex (BIC), which accumulates fluorescently labeled effectors secreted by IH. In each newly entered rice cell, effectors were first secreted into BICs at the tips of the initially filamentous hyphae in the cell. These tip BICs were left behind beside the first-differentiated bulbous IH cells as the fungus continued to colonize the host cell. Fluorescence recovery after photobleaching experiments showed that the effector protein PWL2 (for prevents pathogenicity toward weeping lovegrass [Eragrostis curvula]) continued to accumulate in BICs after IH were growing elsewhere. PWL2 and BAS1 (for biotrophyassociated secreted protein 1), BIC-localized secreted proteins, were translocated into the rice cytoplasm. By contrast, BAS4, which uniformly outlines the IH, was not translocated into the host cytoplasm. Fluorescent PWL2 and BAS1 proteins that reached the rice cytoplasm moved into uninvaded neighbors, presumably preparing host cells before invasion. We report robust assays for elucidating the molecular mechanisms that underpin effector secretion into BICs, translocation to the rice cytoplasm, and cell-to-cell movement in rice.

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“…For example, the aminophospholipid translocase MgApt2 is required for exocytosis during plant infection by the rice blast pathogen Magnaporthe grisea (18). P-type ATPases are a large family of multitransmembrane domain, ATP-dependent transporters, and three subfamilies are found in eukaryotes (29): (i) heavy metal ion ATPases (e.g., copper transporters), (ii) non-heavy-metal ion ATPases (e.g., Ca 2ϩ , H ϩ , Na ϩ , and K ϩ ATPases), and (iii) aminophospholipid translocases (APTs/flippases of the type IV or Drs2 family).…”

mentioning

confidence: 99%

A Putative P-Type ATPase, Apt1, Is Involved in Stress Tolerance and Virulence in Cryptococcus neoformans

Kronstad

2010

Eukaryot Cell

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The export of virulence factors, such as the capsule polysaccharide, to the cell surface is a critical aspect of the pathogenicity of Cryptococcus neoformans. A view of capsule export via exocytosis and extracellular vesicles is emerging, but the molecular mechanisms underlying virulence factor transport pathways remain to be established. In this study, we characterized the APT1 gene, which encodes a predicted integral membrane P-type ATPase belonging to the type IV, Drs2 family of aminophospholipid translocases (flippases) (APTs). APTs maintain the phospholipid asymmetry that is critical in membrane fusion events for trafficking and in establishing cell polarity. Deletion of the APT1 gene resulted in phenotypes consistent with similar roles in C. neoformans. These included altered actin distribution, increased sensitivity to stress conditions (oxidative and nitrosative stress) and to trafficking inhibitors, such as brefeldin A and monensin, a reduction in exported acid phosphatase activity, and hypersensitivity to the antifungal drugs amphotericin B, fluconazole, and cinnamycin. However, there was no difference in growth, capsule size, or melanin production between the wild type and the apt1 mutant strains at either 30°C or 37°C. Despite the absence of an influence on these major virulence factors, Apt1 was required for survival during interactions with macrophages, and apt1 mutants exhibited attenuated virulence in a mouse inhalation model of cryptococcosis. Therefore, Apt1 contributes to virulence and the stress response in C. neoformans through apparent functions in membrane fusion and trafficking that do not influence the deposition of major virulence factors, such as capsule and melanin, outside the cell.The opportunistic fungal pathogen Cryptococcus neoformans causes life-threatening meningoencephalitis in immunocompromised individuals (44). One million cases of cryptococcosis are estimated to occur each year, and approximately two-thirds of these are fatal (43). Key virulence traits for the fungus include growth at the mammalian host temperature, production of a polysaccharide capsule, deposition of laccase-synthesized melanin in the cell wall, secretion of enzymes, and resistance to host defenses, such as oxidative and nitrosative killing (44).The polysaccharide capsule is a key virulence factor and is both cell associated and released during infection (4). The two species of polysaccharide in the capsule, an abundant glucuronoxylomannan (GXM) and a minor galactoxylomannan (GalXM), cause a number of deleterious effects in mammalian hosts (4, 44). Extracellular vesicles (exosomes) containing capsule polysaccharide are present in culture supernatants, in lysates of macrophages containing C. neoformans, and in association with fungal cells during murine infection (41, 49, 50, 54). These so-called "virulence factor delivery bags" are thought to pass through the cell wall to deliver material outside the cell (50). Proteomic analysis of the vesicles identified 76 proteins, and many of these are associated wit...

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A P-type ATPase required for rice blast disease and induction of host resistance

Cited by 98 publications

References 25 publications

Inner workings and biological impact of phospholipid flippases

Inner workings and biological impact of phospholipid flippases

Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

A Putative P-Type ATPase, Apt1, Is Involved in Stress Tolerance and Virulence in Cryptococcus neoformans

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