Furrow-like invaginations of the yeast plasma membrane correspond to membrane compartment of Can1

Strádalová, Vendula; Stahlschmidt, Wiebke; Großmann, Guido; Blažíková, Michaela; Rachel, Reinhard; Tanner, Widmar; Malínský, J

doi:10.1242/jcs.051227

Cited by 151 publications

(220 citation statements)

References 42 publications

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“…Interestingly, the mutants defective in sorting of MCC markers (nce102∆ and pil1∆, see below) did not possess these characteristic structures. Additional experiments, including frequency and distribution analysis and immunolocalization of MCC components, converted this correlation to fairly strong evidence that MCC has an ultrastructural equivalent -furrow-like invaginations of the yeast plasma membrane that had remained mysterious for 46 years [31]. This fact became directly observable on a mutant defective in N-terminal acetylation.…”

Section: Structure Of MCC Patchesmentioning

confidence: 94%

“…The process is reversible, which suggests that the compartment as such is defined by other proteins that are not susceptible to the membrane potential changes. In addition to the H + -symporters above, four proteins of Sur7 family [18,36] and Nce102 with its close homologue Ygr131w [31] were localized in MCC. None of these proteins respond to changes in membrane potential [7,8] and thus, theoretically, they could play the role of those structure-defining elements of MCC.…”

Section: Structure Of MCC Patchesmentioning

confidence: 99%

“…The latter two represent the primary components of eisosome, a newly described organelle [35] situated beneath each of the MCC patches. By immuno-electron microscopy it was shown that Pil1 localizes to the tip of the furrow-like invaginations, the ultrastructural correlates of MCC [31].…”

Section: Structure Of MCC Patchesmentioning

confidence: 99%

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The lateral compartmentation of the yeast plasma membrane

Malínský

Opekarová

Tanner

2010

Yeast

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The plasma membrane of Saccharomyces cerevisiae contains large microdomains enriched in ergosterol, which house at least nine integral proteins, including proton symporters. The domains adopt a characteristic structure of furrow-like invaginations typically seen in freeze-fracture pictures of fungal cells. Being stable for the time comparable with the cell cycle duration, they might be considered as fixed islands (rafts) in an otherwise fluid yeast plasma membrane. Rapidly moving endocytic marker proteins avoid the microdomains; the domain-accumulated proton symporters consequently show a reduced rate of substrate-induced endocytosis and turnover.

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Section: Structure Of MCC Patchesmentioning

confidence: 94%

Section: Structure Of MCC Patchesmentioning

confidence: 99%

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The lateral compartmentation of the yeast plasma membrane

Malínský

Opekarová

Tanner

2010

Yeast

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“…These microcompartments also house two other proton-dependent permeases for uracil and tryptophan, Fur4 and Tat2, respectively, as well as four proteins of the Sur7 family (Young et al , 2002 ;Malinska et al , 2004 ). The MCCs are associated with the eisosomes (discussed below) at the inner leaflet of ergosterol-enriched regions of the plasma membrane, which invaginate in furrow-like structures (Grossmann et al , 2008 ;Stradalova et al , 2009 ). It has been speculated that the transmembrane protein Nce102, which also resides in the MCCs, functions as a sensor to link the membrane ' s sphingolipid content with the formation of the eisosomes (Fr ö hlich et al, 2009 ; see below for more details on the eisosomes).…”

Section: Plasma Membrane Compartmentsmentioning

confidence: 99%

Microcompartments within the yeast plasma membrane

Merzendorfer

Heinisch

2013

Biological Chemistry

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Recent research in cell biology makes it increasingly clear that the classical concept of compartmentation of eukaryotic cells into different organelles performing distinct functions has to be extended by microcompartmentation, i.e., the dynamic interaction of proteins, sugars, and lipids at a suborganellar level, which contributes significantly to a proper physiology. As different membrane compartments (MCs) have been described in the yeast plasma membrane, such as those defined by Can1 and Pma1 (MCCs and MCPs), Saccharomyces cerevisiae can serve as a model organism, which is amenable to genetic, biochemical, and microscopic studies. In this review, we compare the specialized microcompartment of the yeast bud neck with other plasma membrane substructures, focusing on eisosomes, cell wall integrity-sensing units, and chitin-synthesizing complexes. Together, they ensure a proper cell division at the end of mitosis, an intricately regulated process, which is essential for the survival and proliferation not only of fungal, but of all eukaryotic cells.

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“…Such invaginations, also called furrows or troughs, have since been identified in additional freeze fracture EM studies of S. cerevisiae (2)(3)(4)(5)(6) and other fungi (7)(8)(9)(10)(11)(12)(13).…”

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confidence: 96%

Eisosome Ultrastructure and Evolution in Fungi, Microalgae, and Lichens

et al. 2015

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Eisosomes are among the few remaining eukaryotic cellular differentations that lack a defined function(s). These trough-shaped invaginations of the plasma membrane have largely been studied in Saccharomyces cerevisiae, in which their associated proteins, including two BAR domain proteins, have been identified, and homologues have been found throughout the fungal radiation. Using quick-freeze deep-etch electron microscopy to generate high-resolution replicas of membrane fracture faces without the use of chemical fixation, we report that eisosomes are also present in a subset of red and green microalgae as well as in the cysts of the ciliate Euplotes. Eisosome assembly is closely correlated with both the presence and the nature of cell walls. Microalgal eisosomes vary extensively in topology and internal organization. Unlike fungi, their convex fracture faces can carry lineagespecific arrays of intramembranous particles, and their concave fracture faces usually display fine striations, also seen in fungi, that are pitched at lineage-specific angles and, in some cases, adopt a broad-banded patterning. The conserved genes that encode fungal eisosome-associated proteins are not found in sequenced algal genomes, but we identified genes encoding two algal lineage-specific families of predicted BAR domain proteins, called Green-BAR and Red-BAR, that are candidate eisosome organizers. We propose a model for eisosome formation wherein (i) positively charged recognition patches first establish contact with target membrane regions and (ii) a (partial) unwinding of the coiled-coil conformation of the BAR domains then allows interactions between the hydrophobic faces of their amphipathic helices and the lipid phase of the inner membrane leaflet, generating the striated patterns.

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Furrow-like invaginations of the yeast plasma membrane correspond to membrane compartment of Can1

Cited by 151 publications

References 42 publications

The lateral compartmentation of the yeast plasma membrane

The lateral compartmentation of the yeast plasma membrane

Microcompartments within the yeast plasma membrane

Eisosome Ultrastructure and Evolution in Fungi, Microalgae, and Lichens

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