Eisosomes and membrane compartments in the ascomycetes

Scazzocchio, Claudio; Vangelatos, Ioannis; Sophianopoulou, Vicky

doi:10.4161/cib.13764

Cited by 10 publications

(6 citation statements)

References 13 publications

(21 reference statements)

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“…Our results indicate that the composition of MCC/eisosomes in N. crassa is different from that in S. cerevisiae. Apparently MCC/eisosomes' compositions and assembly are dissimilar in different species, which is consistent with published data (Kabeche et al, 2011;Scazzocchio et al, 2011;Douglas and Konopka, 2014). For example, Sur7 and Slm1 were detected as two MCC/eisosomal proteins in budding yeast (Walther et al, 2006;Malinsky and Opekarová, 2016;Busto et al, 2018), and the Sur7 homolog was even examined as a core MCC component, whereas the homologs of Slm1 and Sur7 were not part of MCC/eisosomes in fission yeast (Kabeche et al, 2011).…”

Section: Discussionsupporting

confidence: 89%

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The Composition and the Structure of MCC/Eisosomes in Neurospora crassa

Qin

Kempken

2020

Front. Microbiol.

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MCC/eisosomes are protein-organized domains in the plasma membrane of fungi and algae. However, the composition and function(s) of MCC/eisosomes in the filamentous fungus Neurospora crassa were previously unknown. To identify proteins that localize to MCC/eisosomes in N. crassa, we isolated proteins that co-purified with the core MCC/eisosome protein LSP-1, which was tagged with GFP. Proteins that co-fractionated with LSP-1:GFP were then identified by mass spectrometry. Eighteen proteins were GFP-tagged and used to identify six proteins that highly colocalized with the MCC/eisosome marker LSP-1:RFP, while five other proteins showed partial overlap with MCC/eisosomes. Seven of these proteins showed amino acid sequence homology with proteins known to localize to MCC/eisosomes in the yeast Saccharomyces cerevisiae. However, homologs of three proteins known to localize to MCC/eisosomes in S. cerevisiae (Can1, Pkh1/2, and Fhn1) were not found to colocalize with MCC/eisosome proteins in N. crassa by fluorescence microscopy. Interestingly, one new eisosome protein (glutamine-fructose-6-phosphate aminotransferase, gene ID: NCU07366) was detected in our studies. These findings demonstrate that there are interspecies differences of the protein composition of MCC/eisosomes. To gain further insight, molecular modeling and bioinformatics analysis of the identified proteins were used to propose the organization of MCC/eisosomes in N. crassa. A model will be discussed for how the broad range of functions predicted for the proteins localized to MCC/eisosomes, including cell wall synthesis, response and signaling, transmembrane transport, and actin organization, suggests that MCC/eisosomes act as organizing centers in the plasma membrane.

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Section: Discussionsupporting

confidence: 89%

“…For other fungi, only a few eisosomal proteins have been discovered so far. The eisosome compositions appear to be different in the analyzed fungi (Scazzocchio et al, 2011). In Aspergillus nidulans, PilA, PilB, and SurG were studied and described as core components of MCC/eisosomes (Athanasopoulos et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

The Composition and the Structure of MCC/Eisosomes in Neurospora crassa

Qin

Kempken

2020

Front. Microbiol.

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“…It could also explain why EMCs are necessary for the pathogenicity of fungi in animals and plants (54,55). Since eisosomes are fungus-specific structures (56), they appear to be attractive targets for the development of novel, highly specific antifungals.…”

Section: Discussionmentioning

confidence: 99%

Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains

Gournas

Gkionis

Carquin

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

173

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The eukaryotic plasma membrane is compartmentalized into domains enriched in specific lipids and proteins. However, our understanding of the molecular bases and biological roles of this partitioning remains incomplete. The best-studied domain in yeast is the membrane compartment containing the arginine permease Can1 (MCC) and later found to cluster additional transporters. MCCs correspond to static, furrow-like invaginations of the plasma membrane and associate with subcortical structures named "eisosomes" that include upstream regulators of the target of rapamycin complex 2 (TORC2) in the sensing of sphingolipids and membrane stress. However, how and why Can1 and other nutrient transporters preferentially segregate in MCCs remains unknown. In this study we report that the clustering of Can1 in MCCs is dictated by its conformation, requires proper sphingolipid biosynthesis, and controls its ubiquitin-dependent endocytosis. In the substrate-free outward-open conformation, Can1 accumulates in MCCs in a manner dependent on sustained biogenesis of complex sphingolipids. An arginine transport-elicited shift to an inward-facing conformation promotes its cell-surface dissipation and makes it accessible to the ubiquitylation machinery triggering its endocytosis. We further show that under starvation conditions MCCs increase in number and size, this being dependent on the BAR domain-containing Lsp1 eisosome component. This expansion of MCCs provides protection for nutrient transporters from bulk endocytosis occurring in parallel with autophagy upon TORC1 inhibition. Our study reveals nutrient-regulated protection from endocytosis as an important role for protein partitioning into membrane domains.

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“…Each eisosome contains thousands of copies of Pil1, which can self-assemble into linear tubules and can also generate lipid tubules in vitro (Kabeche et al, 2011;Karotki et al, 2011;Olivera-Couto et al, 2011). Eisosomes and Pil1-related proteins appear to be conserved throughout all ascomycete fungi (Douglas et al, 2011;Olivera-Couto and Aguilar, 2012;Scazzocchio et al, 2011;Ziółkowska et al, 2012). Through studies in many species, it appears that Pil1-assembled eisosomes represent an abundant and prominent structure at the cortex of yeast cells.…”

Section: Introductionmentioning

confidence: 99%

A Pil1-Sle1-Syj1-Tax4 functional pathway links eisosomes with PI(4,5)P2 regulation

Kabeche

Roguev

Krogan

et al. 2014

Journal of Cell Science

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Stable compartments of the plasma membrane promote a wide range of cellular functions. In yeast cells, cytosolic structures called eisosomes generate prominent cortical invaginations of unknown function. Through a series of genetic screens in fission yeast, we found that the eisosome proteins Pil1 and Sle1 function with the synaptojanin-like lipid phosphatase Syj1 and its ligand Tax4. This genetic pathway connects eisosome function with the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P 2 ] in cells. Defects in PI(4,5)P 2 regulation led to eisosome defects, and we found that the core eisosome protein Pil1 can bind to and tubulate liposomes containing PI(4,5)P 2 . Mutations in components of the Pil1-Sle1-Syj1-Tax4 pathway suppress the growth and morphology defects of TORC2 mutants, indicating that eisosome-dependent regulation of PI(4,5)P 2 feeds into signal transduction pathways. We propose that the geometry of membrane invaginations generates spatial and temporal signals for lipid-mediated signaling events in cells.

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Eisosomes and membrane compartments in the ascomycetes

Cited by 10 publications

References 13 publications

The Composition and the Structure of MCC/Eisosomes in Neurospora crassa

The Composition and the Structure of MCC/Eisosomes in Neurospora crassa

Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains

A Pil1-Sle1-Syj1-Tax4 functional pathway links eisosomes with PI(4,5)P2 regulation

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