<i>Aspergillus nidulans</i> BapH is a RAB11 effector that connects membranes in the <scp>S</scp>pitzenkörper with basal autophagy

Pinar, Mario; Peñalva, Miguel

doi:10.1111/mmi.13777

Cited by 13 publications

(16 citation statements)

References 58 publications

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“…These intermediates could be only a subpopulation of each domain, having specialized functions. In support of this, it has been shown that Slm1 of S. cerevisiae and its orthologue SlmA in A. nidulans are not found in all eisosomes or all MCTs, or even all MCL cortical foci (Berchtold et al 2012;Murley et al 2017;Pinar and Peñalva 2017;Busto et al 2018). Further work is needed in order to show whether PM domain intermediates or specialised subpopulations of PM domains exist, which could potentially serve specialized functions.…”

Section: Discussionmentioning

confidence: 99%

“…However, the phylogenetic conservation of such a mechanism is not clear, since the homologues of the Slm proteins in S. pombe do not localize in eisosomes (Kabeche et al 2011). Similarly, SlmA of A. nidulans is only found at the eisosomes of the hyphae (Pinar and Peñalva 2017) and not at those of the head of the germlings, which respond to SL depletion (Athanasopoulos et al 2015). Differences in growth conditions and the existence of different populations of eisosomes with specialized roles (see paragraph 2.1.1) could potentially explain the apparent inconsistences.…”

Section: Mcc-mct -mentioning

confidence: 99%

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Fungal plasma membrane domains

Αθανασόπουλος

André

Sophianopoulou

et al. 2019

FEMS Microbiology Reviews

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The plasma membrane (PM) performs a plethora of physiological processes, the coordination of which requires spatial and temporal organization into specialized domains of different sizes, stability, protein/lipid composition and overall architecture. Compartmentalization of the PM has been particularly well studied in the yeast Saccharomyces cerevisiae, where five non-overlapping domains have been described: The Membrane Compartments containing the arginine permease Can1 (MCC), the H+-ATPase Pma1 (MCP), the TORC2 kinase (MCT), the sterol transporters Ltc3/4 (MCL), and the cell wall stress mechanosensor Wsc1 (MCW). Additional cortical foci at the fungal PM are the sites where clathrin-dependent endocytosis occurs, the sites where the external pH sensing complex PAL/Rim localizes, and sterol-rich domains found in apically grown regions of fungal membranes. In this review, we summarize knowledge from several fungal species regarding the organization of the lateral PM segregation. We discuss the mechanisms of formation of these domains, and the mechanisms of partitioning of proteins there. Finally, we discuss the physiological roles of the best-known membrane compartments, including the regulation of membrane and cell wall homeostasis, apical growth of fungal cells and the newly emerging role of MCCs as starvation-protective membrane domains.

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Section: Discussionmentioning

confidence: 99%

Section: Mcc-mct -mentioning

confidence: 99%

Fungal plasma membrane domains

Αθανασόπουλος

André

Sophianopoulou

et al. 2019

FEMS Microbiology Reviews

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“…BapH is an F‐BAR and PH domain containing protein that holds the honor of being the only bona fide RAB11 effector thus far characterized (Pinar & Peñalva, 2017). The domain composition of BapH suggests that it binds membranes with a certain degree of curvature.…”

Section: The “Canonical” Post‐golgi Rabs: Rab11 and Sec4mentioning

confidence: 99%

The fungal RABOME: RAB GTPases acting in the endocytic and exocytic pathways of Aspergillus nidulans (with excursions to other filamentous fungi)

Pinar

Peñalva

2021

Molecular Microbiology

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RABs (ras-related in brain) comprise a family of small GTPases belonging, with RAS, RHO, RAN, and ARF families to the RAS superfamily (Rojas et al., 2012). RABs were originally described in Saccharomyces cerevisiae, with Ypt1 (the homolog of metazoan RAB1), formerly denoted YPT (for "yeast protein two"), holding the honor of being the first RAB ever identified, and the founding member of the clan (Gallwitz et al., 1983;Schmitt et al., 1986;Segev & Botstein, 1987). Involvement of the yeast exocytic RABs Ypt1 and Sec4 in intracellular traffic was discovered shortly afterwards (Salminen & Novick, 1987;Segev et al., 1988). Meanwhile, genes encoding proteins closely related to yeast YPTs were identified in a rat cDNA library, showing that these GTPases are ubiquitous in eukaryotes (Touchot et al., 1987). In the filamentous fungal world RAB GTPases have been systematically investigated in Aspergillus nidulans, which will be used as guiding thread for this review, with relevant contributions from Ustilago maydis (where the longdistance movement of RAB5 early endosomes (EEs) was originally reported), Magnaporthe oryzae (where Sec4 and its effector, the exocyst, are involved in pathogenesis), and Neurospora crassa (which is well suited to study the spatial regulation of exocytic RABs in the Spitzenkörper), discussed when appropriate.The jungle of gene nomenclature characterizing many fungal papers has also permeated the RAB field. Regretfully, this nomenclature problem jeopardizes literature searches, often impacting

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“…Standard A. nidulans media were used for strain propagation and conidiospore production [49,50]. Genetic techniques have been detailed [51].…”

Section: Aspergillus Media Culture Conditions and Transgenesmentioning

confidence: 99%

Characterization of Aspergillus nidulans TRAPPs uncovers unprecedented similarities between fungi and metazoans and reveals the modular assembly of TRAPPII

et al. 2019

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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 heteroheptamer, 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 sizefractionation 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 composition in mutants lacking essential subunits, which led to the discovery of a stable Trs120/Trs130/Trs65/Tca17 TRAPPII-specific subcomplex whose Trs20-and Trs33-dependent assembly onto core TRAPP generates TRAPPII.

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Aspergillus nidulans BapH is a RAB11 effector that connects membranes in the Spitzenkörper with basal autophagy

Cited by 13 publications

References 58 publications

Fungal plasma membrane domains

Fungal plasma membrane domains

The fungal RABOME: RAB GTPases acting in the endocytic and exocytic pathways of Aspergillus nidulans (with excursions to other filamentous fungi)

Characterization of Aspergillus nidulans TRAPPs uncovers unprecedented similarities between fungi and metazoans and reveals the modular assembly of TRAPPII

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