Vacuolar H+-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger

Schachtschabel, Doreen; Arentshorst, Mark; Lagendijk, Ellen

doi:10.1016/j.fgb.2011.12.008

Cited by 20 publications

(18 citation statements)

References 62 publications

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“…To verify misregulation at the level of protein, we selected a group of SPA-19 regulated genes encoding known cell wall proteins: ncw-7 (Maddi et al, 2009), pir-1 (Mrsa and Tanner, 1999;Mrs a et al, 1997), and phi-a (Schachtschabel et al, 2012). qPCR confirmed RNA-seq data ( Figure 7A), and homologous recombination was used to produced epitope tagged proteins encoded by endogenous loci.…”

Section: Identification Of Spa-19-dependent Genesmentioning

confidence: 98%

Cellular Subcompartments through Cytoplasmic Streaming

et al. 2015

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Cytoplasmic streaming occurs in diverse cell types, where it generally serves a transport function. Here, we examine streaming in multicellular fungal hyphae and identify an additional function wherein regimented streaming forms distinct cytoplasmic subcompartments. In the hypha, cytoplasm flows directionally from cell to cell through septal pores. Using live-cell imaging and computer simulations, we identify a flow pattern that produces vortices (eddies) on the upstream side of the septum. Nuclei can be immobilized in these microfluidic eddies, where they form multinucleate aggregates and accumulate foci of the HDA-2 histone deacetylase-associated factor, SPA-19. Pores experiencing flow degenerate in the absence of SPA-19, suggesting that eddy-trapped nuclei function to reinforce the septum. Together, our data show that eddies comprise a subcellular niche favoring nuclear differentiation and that subcompartments can be self-organized as a consequence of regimented cytoplasmic streaming.

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Section: Identification Of Spa-19-dependent Genesmentioning

confidence: 98%

Cellular Subcompartments through Cytoplasmic Streaming

et al. 2015

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“…Mammalian cells however lack a cell wall, making the fungal cell wall a desirable target for the development of antifungal agents [74, 75]. β-glucan, chitin and mannoproteins are components of the cell wall and disruption of their synthesis can lead to an ineffective cell wall unable to fully protect the cell [76].…”

Section: Fungal Cell Wall As a Drug Development Targetmentioning

confidence: 99%

The Mechanistic Targets of Antifungal Agents: An Overview

Mazu¹,

Bricker²,

Flores‐Rozas³

et al. 2016

MRMC

151

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Pathogenic fungi are a major causative group for opportunistic infections (OIs). AIDS patients and other immunocompromised individuals are at risk for OIs, which if not treated appropriately, contribute to the mortality associated with their conditions. Several studies have indicated that the majority of HIV-positive patients contract fungal infections throughout the course of their disease. Similar observations have been made regarding the increased frequency of bone marrow and organ transplants, the use of antineoplastic agents, the excessive use of antibiotics, and the prolonged use of corticosteroids among others. In addition, several pathogenic fungi have developed resistance to current drugs. Together these have conspired to spur a need for developing new treatment options for OIs. To aid this effort, this article reviews the biological targets of current and emerging drugs and agents that act through these targets for the treatment of opportunistic fungal infections.

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“…The RAVE subunit Rav2p is found only in fungi and does not have human homologs. Therefore, Rav2p offers unique opportunities to selectively disrupt RAVE complex functions in fungal human pathogens for which V-ATPase pumps are desirable targets (65)(66)(67)(68)(69)(70)(71)(72).…”

Section: One "Rave" Path Toward V 1 V O Reassemblymentioning

confidence: 99%

Saccharomyces cerevisiae Vacuolar H ⁺ -ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals

Parra

Chan

2014

Eukaryot Cell

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Vacuolar H؉ -ATPases (V-ATPases) are highly conserved ATP-driven proton pumps responsible for acidification of intracellular compartments. V-ATPase proton transport energizes secondary transport systems and is essential for lysosomal/vacuolar and endosomal functions. These dynamic molecular motors are composed of multiple subunits regulated in part by reversible disassembly, which reversibly inactivates them. Reversible disassembly is intertwined with glycolysis, the RAS/cyclic AMP (cAMP)/ protein kinase A (PKA) pathway, and phosphoinositides, but the mechanisms involved are elusive. The atomic-and pseudoatomic-resolution structures of the V-ATPases are shedding light on the molecular dynamics that regulate V-ATPase assembly. Although all eukaryotic V-ATPases may be built with an inherent capacity to reversibly disassemble, not all do so. V-ATPase subunit isoforms and their interactions with membrane lipids and a V-ATPase-exclusive chaperone influence V-ATPase assembly. This minireview reports on the mechanisms governing reversible disassembly in the yeast Saccharomyces cerevisiae, keeping in perspective our present understanding of the V-ATPase architecture and its alignment with the cellular processes and signals involved. V acuolar Hϩ -ATPases (V-ATPases) are ATP-driven proton pumps distributed throughout the endomembrane system of all eukaryotic cells (1, 2). V-ATPase proton transport acidifies organelles and energizes secondary transport systems. Zymogen activation, protein processing and trafficking, and receptor-mediated endocytosis are fundamental cellular processes that require V-ATPase activity. Cells specialized for active proton secretion express also V-ATPases at the plasma membrane. Proton transport by plasma membrane V-ATPases in osteoclasts, epididymal clear cells, and renal intercalated cells is necessary for bone resorption, sperm maturation, and maintenance of the systemic acidbase balance, respectively (3, 4). V-ATPase has been implicated in several pathological states, including osteopetrosis, distal renal tubular acidosis, male infertility, and cancers (2). Not surprisingly, studies of V-ATPase function and regulation are increasing, as is our knowledge of these dynamic proteins.V-ATPase structure and function are highly conserved and well characterized in Saccharomyces cerevisiae (referred to here as yeast). Lack of V-ATPase function leads to a conditionally lethal phenotype that is characterized by pH sensitivity in yeast; complete lack of V-ATPase function is lethal in higher eukaryotes (5). Recent atomic-and pseudo-atomic-resolution structures of VATPase and its subunits have helped shed light on the molecular dynamics that regulate V-ATPase function (6, 7). V-ATPases are large multisubunit complexes structurally organized into two major domains, V 1 and V o (Fig. 1). Eight peripheral subunits (A to H) form the V 1 domain, where ATP hydrolysis takes place. Six subunits (a, c, c=, cЉ, d, and e) comprise V o , the membrane intrinsic domain that forms the path for proton transport. An impo...

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Vacuolar H+-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger

Cited by 20 publications

References 62 publications

Cellular Subcompartments through Cytoplasmic Streaming

Cellular Subcompartments through Cytoplasmic Streaming

The Mechanistic Targets of Antifungal Agents: An Overview

Saccharomyces cerevisiae Vacuolar H ⁺ -ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals

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Vacuolar H+-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger

Cited by 20 publications

References 62 publications

Cellular Subcompartments through Cytoplasmic Streaming

Cellular Subcompartments through Cytoplasmic Streaming

The Mechanistic Targets of Antifungal Agents: An Overview

Saccharomyces cerevisiae Vacuolar H + -ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals

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Saccharomyces cerevisiae Vacuolar H ⁺ -ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals