Publications
246 results found
Bravo-Plaza I, Tagua VG, Arst HN, et al., 2023, The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain, ELIFE, Vol: 12, ISSN: 2050-084X
Pinar M, Arias-Palomo E, de Los Ríos V, et al., 2019, Characterization of Aspergillus nidulans TRAPPs uncovers unprecedented similarities between fungi and metazoans and reveals the modular assembly of TRAPPII, PLoS Genetics, Vol: 15, ISSN: 1553-7390
TRAnsport Protein Particle complexes (TRAPPs) are ubiquitous regulators of membrane traffic mediating nucleotide exchange on the Golgi regulatory GTPases RAB1 and RAB11. In S. cerevisiae and metazoans TRAPPs consist of two large oligomeric complexes: RAB11-activating TRAPPII and RAB1-activating TRAPPIII. These share a common core TRAPPI hetero-heptamer, absent in metazoans but detected in minor proportions in yeast, likely originating from in vitro-destabilized TRAPPII/III. Despite overall TRAPP conservation, the budding yeast genome has undergone extensive loss of genes, and lacks homologues of some metazoan TRAPP subunits. With nearly twice the total number of genes of S. cerevisiae, another ascomycete Aspergillus nidulans has also been used for studies on TRAPPs. We combined size-fractionation chromatography with single-step purification coupled to mass-spectrometry and negative-stain electron microscopy to establish the relative abundance, composition and architecture of Aspergillus TRAPPs, which consist of TRAPPII and TRAPPIII in a 2:1 proportion, plus a minor amount of TRAPPI. We show that Aspergillus TRAPPIII contains homologues of metazoan TRAPPC11, TRAPPC12 and TRAPPC13 subunits, absent in S. cerevisiae, and establish that these subunits are recruited to the complex by Tca17/TRAPPC2L, which itself binds to the 'Trs33 side' of the complex. Thus Aspergillus TRAPPs compositionally resemble mammalian TRAPPs to a greater extent than those in budding yeast. Exploiting the ability of constitutively-active (GEF-independent, due to accelerated GDP release) RAB1* and RAB11* alleles to rescue viability of null mutants lacking essential TRAPP subunits, we establish that the only essential role of TRAPPs is activating RAB1 and RAB11, and genetically classify each essential subunit according to their role(s) in TRAPPII (TRAPPII-specific subunits) or TRAPPII and TRAPPIII (core TRAPP subunits). Constitutively-active RAB mutant combinations allowed examination of TRAPP comp
Hernandez-Gonzalez M, Bravo-Plaza I, Pinar M, et al., 2018, Endocytic recycling via the TGN underlies the polarized hyphal mode of growth, PLoS Genetics, Vol: 14, ISSN: 1553-7390
Intracellular traffic in Aspergillus nidulans hyphae must cope with the challenges that the high rates of apical extension (1μm/min) and the long intracellular distances (>100 μm) impose. Understanding the ways in which the hyphal tip cell coordinates traffic to meet these challenges is of basic importance, but is also of considerable applied interest, as fungal invasiveness of animals and plants depends critically upon maintaining these high rates of growth. Rapid apical extension requires localization of cell-wall-modifying enzymes to hyphal tips. By combining genetic blocks in different trafficking steps with multidimensional epifluorescence microscopy and quantitative image analyses we demonstrate that polarization of the essential chitin-synthase ChsB occurs by indirect endocytic recycling, involving delivery/exocytosis to apices followed by internalization by the sub-apical endocytic collar of actin patches and subsequent trafficking to TGN cisternae, where it accumulates for ~1 min before being re-delivered to the apex by a RAB11/TRAPPII-dependent pathway. Accordingly, ChsB is stranded at the TGN by Sec7 inactivation but re-polarizes to the apical dome if the block is bypassed by a mutation in geaAgea1 that restores growth in the absence of Sec7. That polarization is independent of RAB5, that ChsB predominates at apex-proximal cisternae, and that upon dynein impairment ChsB is stalled at the tips in an aggregated endosome indicate that endocytosed ChsB traffics to the TGN via sorting endosomes functionally located upstream of the RAB5 domain and that this step requires dynein-mediated basipetal transport. It also requires RAB6 and its effector GARP (Vps51/Vps52/Vps53/Vps54), whose composition we determined by MS/MS following affinity chromatography purification. Ablation of any GARP component diverts ChsB to vacuoles and impairs growth and morphology markedly, emphasizing the important physiological role played by this pathway that, we propose, is ce
López-Berges MS, Arst HN, Pinar M, et al., 2017, Genetic studies on the physiological role of CORVET in Aspergillus nidulans., FEMS Microbiology Letters, Vol: 364, ISSN: 0378-1097
CORVET and HOPS are protein complexes mediating the maturation of early endosomes (EEs) into late endosomes (LEs)/vacuoles. These hetero-hexamers share four 'core' components, Vps11, Vps16, Vps18 and Vps33, and differ in two specific subunits, CORVET Vps8 and Vps3 and HOPS Vps39 and Vps41. Whereas ablating HOPS-specific components has minor growth effects, ablating any CORVET constituent severely debilitates Aspergillus nidulans growth, buttressing previous work indicating that maturation of EEs into LEs is physiologically crucial. A genetic screen revealed that impairing the slt cation homeostasis pathway rescues the growth defect resulting from inactivation of the 'core' protein Vps33. Subsequent genetic analyses showed that the defect resulting from lack of any one of the five other CORVET components could similarly be rescued by sltAΔ eliminating the slt regulator SltA. Whereas double deletants lacking functionally non-equivalent components of the CORVET and HOPS complexes are rescued by sltAΔ, those lacking functionally equivalent components are not, suggesting that intermediate 'hybrid' complexes previously detected in yeast are physiologically relevant. vps3Δ, vps8Δ, vps39Δ and vps41Δ result in small vacuoles. This phenotype is remediable by sltAΔ in the case of CORVET-specific, but not in the case of HOPS-specific deletants, indicating that the slt- effect on vacuolar size necessitates HOPS.
Arst HN, Mellado L, Espeso EA, 2016, Proteolytic activation of both components of the cation-stress responsive Slt pathway in Aspergillus nidulans, Molecular Biology of the Cell, Vol: 27, Pages: 2598-2612, ISSN: 1939-4586
Tolerance of Aspergillus nidulans to alkalinity and elevated cation concentrations requires both SltA and SltB. Transcription factor SltA and the putative pseudo-kinase/protease signaling protein SltB comprise a regulatory pathway specific to filamentous fungi. In vivo SltB is proteolytically cleaved into its two principal domains. Mutational analysis defines a chymotrypsin-like serine protease domain that mediates SltB auto-proteolysis and the proteolytic cleavage of SltA. The pseudo-kinase domain might modulate the protease activity of SltB. Three forms of the SltA transcription factor coexist in cells, a full-length 78kDa version and a processed 32kDa form which is found in phosphorylated and unphosphorylated states. The SltA32kDa version mediates transcriptional regulation of sltB and, putatively, genes required for tolerance to cation stress and alkalinity. The full length form SltA78kDa apparently has no transcriptional function. In the absence of SltB only the primary product of SltA is detectable and its level equals that of SltA78kDa. Mutations in sltB selected as suppressors of null vps alleles and resulting in cation/alkalinity sensitivity either reduced or eliminated SltA proteolysis. There is no evidence for cation or alkalinity regulation of SltB cleavage, but activation of sltB expression requires SltA. This work identifies the molecular mechanisms governing the Slt pathway.
Arst HN, Lucena-Agell D, Hervas-Aguilar A, et al., 2016, Mutational analysis of the Aspergillus ambient pH receptor PalH underscores its potential as a target for antifungal compounds, Molecular Microbiology, Vol: 101, Pages: 982-1002, ISSN: 0950-382X
The pal/RIM ambient pH signalling pathway is crucial for the ability of pathogenic fungi to infect hosts. The Aspergillus nidulans 7‐TMD receptor PalH senses alkaline pH, subsequently facilitating ubiquitination of the arrestin PalF. Ubiquitinated PalF triggers downstream signalling events. The mechanism(s) by which PalH transduces the alkaline pH signal to PalF is poorly understood. We show that PalH is phosphorylated in a signal dependent manner, resembling mammalian GPCRs, although PalH phosphorylation, in contrast to mammalian GPCRs, is arrestin dependent. A genetic screen revealed that an ambient‐exposed region comprising the extracellular loop connecting TM4‐TM5 and ambient‐proximal residues within TM5 is required for signalling. In contrast, substitution by alanines of four aromatic residues within TM6 and TM7 results in a weak ‘constitutive’ activation of the pathway. Our data support the hypothesis that PalH mechanistically resembles mammalian GPCRs that signal via arrestins, such that the relative positions of individual helices within the heptahelical bundle determines the Pro316‐dependent transition between inactive and active PalH conformations, governed by an ambient‐exposed region including critical Tyr259 that potentially represents an agonist binding site. These findings open the possibility of screening for agonist compounds stabilizing the inactive conformation of PalH, which might act as antifungal drugs against ascomycetes.v
López-Berges MS, Pinar M, Abenza JF, et al., 2016, The Aspergillus nidulans syntaxin PepA(Pep12) is regulated by two Sec1/Munc-18 proteins to mediate fusion events at early endosomes, late endosomes and vacuoles., Molecular Microbiology, Vol: 99, Pages: 199-216, ISSN: 1365-2958
Syntaxins are target-SNAREs that crucially contribute to determine membrane compartment identity. Three syntaxins, Tlg2p, Pep12p and Vam3p organize the yeast endovacuolar system. Remarkably, filamentous fungi lack the equivalent of the yeast vacuolar syntaxin Vam3p, making unclear how these organisms regulate vacuole fusion. We show that the nearly essential A. nidulans syntaxin PepA(Pep12) , present in all endocytic compartments between early endosomes and vacuoles, shares features of Vam3p and Pep12p, and is capable of forming compositional equivalents of all known yeast endovacuolar SNARE bundles including that formed by yeast Vam3p for vacuolar fusion. Our data further indicate that regulation by two Sec1/Munc-18 proteins, Vps45 in early endosomes, and Vps33 in early and late endosomes/vacuoles, contributes to the wide domain of PepA(Pep12) action. The syntaxin TlgB(Tlg2) localizing to the TGN appears to mediate retrograde traffic connecting post-Golgi (sorting) endosomes with the TGN. TlgB(Tlg2) is dispensable for growth but becomes essential if the early Golgi syntaxin SedV(Sed5) is compromised, showing that the Golgi can function with a single syntaxin, SedV(Sed5) . Remarkably, its pattern of associations with endosomal SNAREs is consistent with SedV(Sed5) playing roles in retrograde pathway(s) connecting endocytic compartments downstream of the post-Golgi endosome with the Golgi, besides more conventional intra-Golgi roles.
Arst HN, Bussink H-J, Bignell EM, et al., 2015, Refining the pH response in Aspergillus nidulans: a modulatory triad involving PacX, a novel zinc binuclear cluster protein, Molecular Microbiology, Vol: 98, Pages: 1051-1072, ISSN: 1365-2958
The Aspergillus nidulans PacC transcription factor mediates gene regulation in response to alkaline ambient pH which, signalled by the Pal pathway, results in the processing of PacC⁷² to PacC²⁷ via PacC⁵³. Here we investigate two levels at which the pH regulatory system is transcriptionally moderated by pH and identify and characterise a new component of the pH regulatory machinery, PacX. Transcript level analysis and overexpression studies demonstrate that repression of acid-expressed palF, specifying the Pal pathway arrestin, probably by PacC²⁷ and/or PacC⁵³, prevents an escalating alkaline pH response. Transcript analyses using a reporter and constitutively expressed pacC trans-alleles show that pacC preferential alkaline-expression results from derepression by depletion of the acid-prevalent PacC⁷² form. We additionally show that pacC repression requires PacX. pacX mutations suppress PacC processing recalcitrant mutations, in part, through derepressed PacC levels resulting in traces of PacC²⁷ formed by pH-independent proteolysis. pacX was cloned by impala transposon mutagenesis. PacX, with homologues within the Leotiomyceta, has an unusual structure with an amino-terminal coiled-coil and a carboxy-terminal zinc binuclear cluster. pacX mutations indicate the importance of these regions. One mutation, an unprecedented finding in A. nidulans genetics, resulted from an insertion of an endogenous Fot1-like transposon.
Yao X, Arst HN, Wang X, et al., 2015, Discovery of a vezatin-like protein for dynein-mediated early endosome transport., Molecular Biology of the Cell, Vol: 26, Pages: 3816-3827, ISSN: 1939-4586
Early endosomes are transported bidirectionally by cytoplasmic dynein and kinesin-3, but how the movements are regulated in vivo remains unclear. Here our forward genetic study led to the discovery of VezA, a vezatin-like protein in Aspergillus nidulans, as a factor critical for early endosome distribution. Loss of vezA causes an abnormal accumulation of early endosomes at the hyphal tip where microtubule plus ends are located. This abnormal accumulation depends on kinesin-3 and is due to a decrease in the frequency but not the speed of dynein-mediated early endosome movement. VezA-GFP signals are enriched at the hypha tip in an actin-dependent manner, but are not obviously associated with early endosomes, thus differing from the early endosome association of the cargo adapter HookA (Hook in A. nidulans). On loss of VezA, HookA associates normally with early endosomes but the interaction between dynein-dynactin and the early-endosome-bound HookA is significantly decreased. However, VezA is not required for linking dynein-dynactin to the cytosolic ∆C-HookA, lacking the cargo-binding C-terminus. These results identify VezA as a novel regulator required for the interaction between dynein and the Hook-bound early endosomes in vivo.
Arst HN, Mellado L, Calcagno-Pizarelli AM, et al., 2015, A second component of the SltA-dependent cation tolerance pathway in Aspergillus nidulans, Fungal Genetics and Biology, Vol: 82, Pages: 116-128, ISSN: 1096-0937
Xiang X, Qiu R, Yao X, et al., 2015, Cytoplasmic dynein and early endosome transport, Cellular and Molecular Life Sciences, Vol: 72, Pages: 3267-3280, ISSN: 1420-9071
Microtubule-based distribution of organelles/vesicles is crucial for the function of many types of eukaryotic cells and the molecular motor cytoplasmic dynein is required for transporting a variety of cellular cargos toward the microtubule minus ends. Early endosomes represent a major cargo of dynein in filamentous fungi, and dynein regulators such as LIS1 and the dynactin complex are both required for early endosome movement. In fungal hyphae, kinesin-3 and dynein drive bi-directional movements of early endosomes. Dynein accumulates at microtubule plus ends; this accumulation depends on kinesin-1 and dynactin, and it is important for early endosome movements towards the microtubule minus ends. The physical interaction between dynein and early endosome requires the dynactin complex, and in particular, its p25 component. The FTS-Hook-FHIP (FHF) complex links dynein–dynactin to early endosomes, and within the FHF complex, Hook interacts with dynein–dynactin, and Hook-early endosome interaction depends on FHIP and FTS.
Pinar M, Arst HN, Pantazopoulou A, et al., 2015, TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabE<SUP>RAB11</SUP>, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 112, Pages: 4346-4351, ISSN: 0027-8424
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- Citations: 49
Lucena-Agell D, Galindo A, Arst HN, et al., 2015, Aspergillus nidulans ambient pH signaling does not require endocytosis, Eukaryotic Cell, Vol: 14, Pages: 545-553, ISSN: 1535-9778
Aspergillus nidulans (Pal) ambient pH signaling takes place in cortical structures containing components of the ESCRT pathway, which are hijacked by the alkaline pH-activated, ubiquitin-modified version of the arrestin-like protein PalF and taken to the plasma membrane. There, ESCRTs scaffold the assembly of dedicated Pal proteins acting downstream. The molecular details of this pathway, which results in the two-step proteolytic processing of the transcription factor PacC, have received considerable attention due to the key role that it plays in fungal pathogenicity. While current evidence strongly indicates that the pH signaling role of ESCRT complexes is limited to plasma membrane-associated structures where PacC proteolysis would take place, the localization of the PalB protease, which almost certainly catalyzes the first and only pH-regulated proteolytic step, had not been investigated. In view of ESCRT participation, this formally leaves open the possibility that PalB activation requires endocytic internalization. As endocytosis is essential for hyphal growth, nonlethal endocytic mutations are predicted to cause an incomplete block. We used a SynA internalization assay to measure the extent to which any given mutation prevents endocytosis. We show that none of the tested mutations impairing endocytosis to different degrees, including slaB1, conditionally causing a complete block, have any effect on the activation of the pathway. We further show that PalB, like PalA and PalC, localizes to cortical structures in an alkaline pH-dependent manner. Therefore, signaling through the Pal pathway does not involve endocytosis.
Arst HN, Hernandez-Gonzalez M, Penalva MA, et al., 2014, GBF/Gea mutant with a single substitution sustains fungal growth in the absence of BIG/Sec7, FEBS LETTERS, Vol: 588, Pages: 4799-4806, ISSN: 0014-5793
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- Citations: 14
Penalva MA, Lucena-Agell D, Arst HN, 2014, <i>Liaison alcaline</i>: Pals entice non-endosomal ESCRTs to the plasma membrane for pH signaling, CURRENT OPINION IN MICROBIOLOGY, Vol: 22, Pages: 49-59, ISSN: 1369-5274
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- Citations: 47
Yao X, Arst HN, Wang X, et al., 2014, VezA, a novel factor required for dynein-mediated early endosome transport., ASCB/IFCB Meeting, Publisher: AMER SOC CELL BIOLOGY, ISSN: 1059-1524
Zhang J, Qiu R, Arst HN, et al., 2014, HookA is a novel dynein-early endosome linker critical for cargo movement in vivo, JOURNAL OF CELL BIOLOGY, Vol: 204, Pages: 1009-1026, ISSN: 0021-9525
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- Citations: 84
Almeida RS, Loss O, Colabardini AC, et al., 2013, Genetic Bypass of <i>Aspergillus nidulans crzA</i> Function in Calcium Homeostasis, G3-GENES GENOMES GENETICS, Vol: 3, Pages: 1129-1141, ISSN: 2160-1836
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- Citations: 8
Pinar M, Pantazopoulou A, Arst HN, et al., 2013, Acute inactivation of the <i>Aspergillus nidulans</i> Golgi membrane fusion machinery: correlation of apical extension arrest and tip swelling with cisternal disorganization, MOLECULAR MICROBIOLOGY, Vol: 89, Pages: 228-248, ISSN: 0950-382X
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- Citations: 48
Zhang J, Qiu R, Arst HN, et al., 2013, A Hook protein links cytoplasmic dynein to early endosomes for dynein-driven early endosome movement, MOLECULAR BIOLOGY OF THE CELL, Vol: 24, ISSN: 1059-1524
Apostolaki A, Harispe L, Calcagno-Pizarelli AM, et al., 2012, Aspergillus nidulans CkiA is an essential casein kinase I required for delivery of amino acid transporters to the plasma membrane, MOLECULAR MICROBIOLOGY, Vol: 84, Pages: 530-549, ISSN: 0950-382X
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- Citations: 28
Galindo A, Calcagno-Pizarelli AM, Arst HN, et al., 2012, An ordered pathway for the assembly of fungal ESCRT-containing ambient pH signalling complexes at the plasma membrane, JOURNAL OF CELL SCIENCE, Vol: 125, Pages: 1784-1795, ISSN: 0021-9533
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- Citations: 60
Peñalva MA, Galindo A, Abenza JF, et al., 2012, Searching for gold beyond mitosis: Mining intracellular membrane traffic in Aspergillus nidulans., Cell Logist, Vol: 2, Pages: 2-14, ISSN: 2159-2780
The genetically tractable filamentous ascomycete fungus Aspergillus nidulans has been successfully exploited to gain major insight into the eukaryotic cell cycle. More recently, its amenability to in vivo multidimensional microscopy has fueled a potentially gilded second age of A. nidulans cell biology studies. This review specifically deals with studies on intracellular membrane traffic in A. nidulans. The cellular logistics are subordinated to the needs imposed by the polarized mode of growth of the multinucleated hyphal tip cells, whereas membrane traffic is adapted to the large intracellular distances. Recent work illustrates the usefulness of this fungus for morphological and biochemical studies on endosome and Golgi maturation, and on the role of microtubule-dependent motors in the long-distance movement of endosomes. The fungus is ideally suited for genetic studies on the secretory pathway, as mutations impairing secretion reduce apical extension rates, resulting in phenotypes detectable by visual inspection of colonies.
Calcagno-Pizarelli AM, Hervas-Aguilar A, Galindo A, et al., 2011, Rescue of <i>Aspergillus nidulans</i> severely debilitating null mutations in ESCRT-0, I, II and III genes by inactivation of a salt-tolerance pathway allows examination of ESCRT gene roles in pH signalling, JOURNAL OF CELL SCIENCE, Vol: 124, Pages: 4064-4076, ISSN: 0021-9533
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- Citations: 26
Findon H, Calcagno-Pizarelli AM, Martínez JL, et al., 2010, Analysis of a novel calcium auxotrophy in Aspergillus nidulans., Fungal Genet Biol, Vol: 47, Pages: 647-655, ISSN: 1096-0937
In Aspergillus nidulans a combination of null mutations in halA, encoding a protein kinase, and sltA, encoding a zinc-finger transcription factor having no yeast homologues, results in an elevated calcium requirement ('calcium auxotrophy') without impairing net calcium uptake. sltA(-) (+/-halA(-)) mutations result in hypertrophy of the vacuolar system. In halA(-)sltA(-) (and sltA(-)) strains, transcript levels for pmcA and pmcB, encoding vacuolar Ca(2+)-ATPase homologues, are highly elevated, suggesting a regulatory relationship between vacuolar membrane area and certain vacuolar membrane ATPase levels. Deletion of both pmcA and pmcB strongly suppresses the 'calcium auxotrophy'. Therefore the 'calcium auxotrophy' possibly results from excessive vacuolar calcium sequestration, causing cytosolic calcium deprivation. Null mutations in nhaA, homologous to Saccharomyces cerevisiae NHA1, encoding a plasma membrane Na(+)/H(+) antiporter effluxing Na(+) and K(+), and a non-null mutation in trkB, homologous to S. cerevisiae TRK1, encoding a plasma membrane high affinity K(+) transporter, also suppress the calcium auxotrophy.
Hervás-Aguilar A, Rodríguez-Galán O, Galindo A, et al., 2010, Characterization of Aspergillus nidulans DidB Did2, a non-essential component of the multivesicular body pathway., Fungal Genet Biol, Vol: 47, Pages: 636-646, ISSN: 1087-1845
ESCRT-III heteropolymers mediate membrane protein cargo sorting into multivesicular endosomes for subsequent vacuolar degradation. We studied the localization of largely uncharacterized Aspergillus nidulans ESCRT-III using its key structural component Vps32 and the 'associated' component DidB(Did2). Vps32-GFP localizes to motile early endosomes as reported, but predominates in aggregates often associated with vacuoles due to inability to dissociate from endosomes. DidB(Did)(2) regulating Vps4 (the ATPase disassembling ESCRT-III) is not essential. Consistent with this accessory role, didB Delta is unable to block the MVB sorting of the glutamate transporter AgtA, but increases its steady-state level and mislocalizes a fraction of the permease to the plasma membrane under conditions promoting its vacuolar targeting. didB Delta exacerbates the dominant-negative growth defect resulting from Vps32-GFP over-expression. A proportion of DidB-GFP is detectable in early endosomes colocalizing with RabA(Rab5) and accumulating in nudA1 tips, suggesting that ESCRT-III assembles on endosomes from the early steps of the endocytic pathway.
Tilburn J, Arst H, Peñalva MA, 2010, Regulation of Gene Expression by Ambient pH, Cellular and Molecular Biology of Filamentous Fungi, Editors: Borkovich, Ebbole, USA, Publisher: American Society for Microbiology, USA
Rodriguez-Galan O, Galindo A, Hervas-Aguilar A, et al., 2009, Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of <i>Aspergillus</i> PalB Cysteine Protease to ESCRT-III, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 284, Pages: 4404-4412
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- Citations: 46
Spielvogel A, Findon H, Arst HN, et al., 2008, Two zinc finger transcription factors, CrzA and SltA, are involved in cation homoeostasis and detoxification in <i>Aspergillus nidulans</i>, BIOCHEMICAL JOURNAL, Vol: 414, Pages: 419-429, ISSN: 0264-6021
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- Citations: 91
Penalva MA, Tilburn J, Bignell E, et al., 2008, Ambient pH gene regulation in fungi: making connections, TRENDS IN MICROBIOLOGY, Vol: 16, Pages: 291-300, ISSN: 0966-842X
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- Citations: 276
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