Sterol glucosyltransferases have different functional roles in<i>Pichia pastoris</i> and <i>Yarrowia lipolytica</i>

Stasyk, Oleh; Nazarko, Taras Y.; Krasovska, Olena S.; Warnecke, Dirk; Nicaud, Jean‐Marc; Cregg, James M.; Sibirny, Andriy А.

doi:10.1016/j.cellbi.2003.08.004

Cited by 41 publications

(45 citation statements)

References 18 publications

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“…The Atg26 protein, encoding a uridine-diphosphateglucose:sterol glucosyltransferase, is required uniquely for both macro-and micropexophagy but not for starvationinduced macroautophagy in P. pastoris, or for pexophagy in Yarrowia lipolytica [44,61]. This protein has a pleckstrin homology (PH), GRAM (glucosyltransferases, Rab-like GTPase activators, and myotubularins) and a catalytic domain, all three of which are needed for micropexophagy.…”

Section: Micropexophagymentioning

confidence: 99%

Peroxisome turnover by micropexophagy: an autophagy-related process

Farré

Subramani

2004

Trends in Cell Biology

153

133

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Many organisms stringently regulate the number, volume and enzymatic content of peroxisomes (and other organelles). Understanding this regulation requires knowledge of how organelles are assembled and selectively destroyed in response to metabolic cues. In the past decade, considerable progress has been achieved in the elucidation of the roles of genes involved in peroxisome biogenesis, half of which are affected in human peroxisomal disorders. The recent discovery of intermediates and genes in peroxisome turnover by selective autophagy-related processes (pexophagy) opens the door to understanding peroxisome turnover and homeostasis. In this article, we summarize advances in the characterization of genes that are necessary for the transport and delivery of selective and nonselective cargos to the lysosome or vacuole by autophagy-related processes, with emphasis on peroxisome turnover by micropexophagy.During autophagy, cargos consisting of individual proteins, bulk cytosol and/or subcellular organelles, are degraded in the lysosome (or vacuole in yeast), with ensuing recycling of the amino acid and lipid precursors. Although autophagy was thought initially to enable cells to survive nutrient starvation by degradation and recycling of dispensable cellular components, it is now recognized to be involved in a plethora of cellular responses, including the regulation of organelle number [1][2][3] Autophagy is universal to all eukaryotic cells, including yeasts, worms, insects, plants and mammals [10]. In unicellular organisms, such as yeasts, it is observed primarily under nutrient starvation conditions or during the re-adaptation of cells switched from certain environments to others. Two morphologically distinct, but mechanistically related, forms of autophagy common to uni-and multicellular eukaryotes have been described. These are macroautophagy and microautophagy (Figure 1). A third form, called chaperone-mediated autophagy, has been found only in mammalian systems and is described elsewhere [9]. Autophagy is often a degradative process but it can be either selective or nonselective with respect to cargo that is turned over. The degradation of nonselective cargo is a mechanism for recycling any excess cellular components (e.g. cytosol and/or organelles) and might be a strategy for adaptation to different environments. By contrast, cells resort to selective autophagic turnover of nonfunctional or damaged organelles, or protein aggregates, that might be too large for other proteolysis machinery, such as the proteasome.Unlike the autophagic pathways, the related cytosol-tovacuole transport (Cvt) pathway, described to date only in Saccharomyces cerevisiae, delivers a limited set of specific, Morphological steps in the cytosol-to-vacuole transport (Cvt), macroautophagy and microautophagy pathways in yeast. In microautophagy, organelles and/or cytosolic proteins are engulfed by the vacuolar membrane in a Pac-Manelike fashion and degraded in the vacuolar lumen. Macroautophagy involves the formation of large (300-900 nm)...

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Section: Micropexophagymentioning

confidence: 99%

Peroxisome turnover by micropexophagy: an autophagy-related process

Farré

Subramani

2004

Trends in Cell Biology

153

133

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“…4 However, in the alkane-utilizing yeast Yarrowia lipolytica, it is not required for pexophagy. 6 Because the S. cerevisiae Atg26 protein (ScAtg26) possesses all three, PH, GRAM, and UDPGT, domains, which share significant sequence identities, 46%, 43.3% and 62.5% respectively, with those in PpAtg26, we were interested to know whether the ScAtg26 function was conserved. In this study, we determined the involvement of ScAtg26 in the Cvt pathway, macroautophagy and pexophagy.…”

Section: Introductionmentioning

confidence: 99%

Atg26 is Not Involved in Autophagy-Related Pathways inSaccharomyces cerevisiae

Cao¹,

Klionsky²

2007

Autophagy

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Previously published online a an Autophagy E-publication: http://www.landesbioscience.com/journals/autophagy/abstract.php?id=3371 KEY WORDScytoplasm to vacuole targeting, lysosome, pexophagy, protein transport, vacuole, yeast Atg26 is Not Involved in Autophagy-Related Pathways in Saccharomyces cerevisiae ABSTRACTAutophagy is a degradative pathway conserved among eukaryotes. It is a major route for degradation of long-lived proteins and entire organelles, such as peroxisomes. Atg26, a sterol glucosyltransferase, is specifically required for micro-and macropexophagy, but not for starvation-induced bulk autophagy in Pichia pastoris. Here we study the requirement of Saccharomyces cerevisiae Atg26 in the Cvt pathway, nonspecific autophagy and pexophagy. Our results show that the S. cerevisiae atg26∆ strain is not defective in prApe1 maturation, macroautophagy or peroxisome degradation, in contrast to the situation seen in Pichia pastoris. These studies highlight the importance of examining mutants in multiple organisms.

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“…They also showed that GlcSte accumulates in one strain of P. pastoris in response to heat or ethanol shock, in contrast to GlcCer, which appears to be constitutively expressed. The evidence suggests that GlcSte is not essential for viability, although UGT51p-catalyzed biosynthesis of GlcSte was recently shown to be required for oxidative metabolism of small molecules, such as methanol or alkanes, by some fungi (36,37).…”

Section: Discussionmentioning

confidence: 99%

Neutral glycolipids of the filamentous fungus Neurospora crassa:altered expression in plant defensin-resistant mutants

Park

Bennion

François

et al. 2005

Journal of Lipid Research

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. For this study, neutral glycolipid components were extracted from wild-type and plant defensin-resistant mutant strains of N. crassa . The structures of purified components were elucidated by NMR spectroscopy and mass spectrometry. Neutral glycosphingolipids of both wild-type and mutant strains were characterized as ␤ -glucopyranosylceramides, but those of the mutants were found with structurally altered ceramides. Although the wild type expressed a preponderance of N -2 -hydroxy-( E )-⌬ 3 -octadecenoate as the fatty-N -acyl component attached to the long-chain base (4 E ,8 E )-9-methyl-4,8-sphingadienine, the mutant ceramides were found with mainly N -2 -hydroxyhexadecanoate instead. In addition, the mutant strains expressed highly increased levels of a sterol glucoside identified as ergosterol-␤ -glucoside. The potential implications of these findings with respect to defensin resistance in the N. crassa mutants are discussed.

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Sterol glucosyltransferases have different functional roles inPichia pastoris and Yarrowia lipolytica

Cited by 41 publications

References 18 publications

Peroxisome turnover by micropexophagy: an autophagy-related process

Peroxisome turnover by micropexophagy: an autophagy-related process

Atg26 is Not Involved in Autophagy-Related Pathways inSaccharomyces cerevisiae

Neutral glycolipids of the filamentous fungus Neurospora crassa:altered expression in plant defensin-resistant mutants

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