The Notch signalling regulator Fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DxD

Munro, Sean; Freeman, Matthew

doi:10.1016/s0960-9822(00)00578-9

Cited by 179 publications

(119 citation statements)

References 48 publications

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“…A punctate staining throughout the cytoplasm ( Figure 3A), characteristic of the Golgi apparatus in Drosophila tissues was observed (Ripoche et al, 1994;Stanley et al, 1997;Rabouille et al, 1999;Lecuit and Wieschaus, 2000;Munro and Freeman, 2000;Sisson et al, 2000). This pattern is different from mammalian cells and is more reminiscent of a plant or yeast Golgi pattern .…”

Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 86%

“…These flies carry the transgene comprising the Fringe cDNA in which the glycosyltransferase motif DDD motif has been replaced by a DXD that abolishes the glycosyltransferase activity but retains the Golgi localization (Munro and Freeman, 2000). Female flies were crossed to HsGAL4/Bc, El, Gla.…”

Section: Fly Stocks and Experimentsmentioning

confidence: 99%

“…The glycosyltransferase Fringe has recently been shown to be a Golgi protein (Bruckner et al, 2000;Munro and Freeman, 2000). Transgenic flies carrying UAS-Fringe-DXD tagged with the myc epitope provided us with an alternative tool to confirm the Golgi nature of the disc larval clusters.…”

Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 99%

“…Transgenic flies carrying UAS-Fringe-DXD tagged with the myc epitope provided us with an alternative tool to confirm the Golgi nature of the disc larval clusters. Fringe localization in the fly Golgi apparatus was shown to be unaffected when the glycosyltransferase motif DDD was changed to DXD (Munro and Freeman, 2000). Fringe-DXDmyc was expressed ubiquitously at low level (see MATERI-ALS AND METHODS) and with the use of 9E10 (a monoclonal anti-myc antibody) on sections of unicryl-embedded discs, it was localized to larval clusters (Figure 4, A and B) and Golgi stacks ( Figure 4C) when present (the heat shock necessary to induce Fringe expression has driven some of the clusters to be converted into stacks, see below; Figure 7B).…”

Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 99%

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Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

Kondylis

Goulding

Dunne

et al. 2001

MBoC

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We provide a detailed description of Golgi stack biogenesis that takes place in vivo during one of the morphogenetic events in the lifespan of Drosophila melanogaster. In early third-instar larvae, small clusters consisting mostly of vesicles and tubules were present in epithelial imaginal disk cells. As larvae progressed through mid-and late-third instar, these larval clusters became larger but also increasingly formed cisternae, some of which were stacked. In white pupae, the typical Golgi stack was observed. We show that larval clusters are Golgi stack precursors by 1) localizing various Golgi-specific markers to the larval clusters by electron and immunofluorescence confocal microscopy, 2) driving this conversion in wild-type larvae incubated at 37°C for 2 h, and 3) showing that this conversion does not take place in an NSF1 mutant (comt 17). The biological significance of this conversion became clear when we found that the steroid hormone 20-hydroxyecdysone (ecdysone) is critically involved in this conversion. In its absence, Golgi stack biogenesis did not occur and the larval clusters remained unaltered. We showed that dGM130 and sec23p expression increases approximately three-and fivefold, respectively, when discs are exposed to ecdysone in vivo and in vitro. Taken together, these results suggest that we have developed an in vivo system to study the ecdysone-triggered Golgi stack biogenesis.

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Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 86%

Section: Fly Stocks and Experimentsmentioning

confidence: 99%

Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 99%

Section: Larval Clusters Contain Golgi Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

Kondylis

Goulding

Dunne

et al. 2001

MBoC

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“…Structural studies on a number of enzymes have shown that these aspartate residues coordinate the Mn 2ϩ ion that plays a central role in catalysis (31)(32)(33)(34). Moreover, the aspartates have been shown to necessary for the activity of a wide range of glycosyltransferases (29,(35)(36)(37)(38). In this paper we determine the stoichiometry of Mnn9p and Van1p in M-Pol I, and use mutations in their DXD motifs to investigate in vivo and in vitro the contribution the two proteins make to the activity of the complex.…”

mentioning

confidence: 99%

The Components of the Saccharomyces cerevisiaeMannosyltransferase Complex M-Pol I Have Distinct Functions in Mannan Synthesis

Stolz

Munro

2002

Journal of Biological Chemistry

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The yeast Saccharomyces cerevisiae processes N-linked glycans in the Golgi apparatus in two different ways. Whereas most of the proteins of internal membranes receive a simple core-type structure, a long branched polymer termed mannan is attached to the glycans of many of the proteins destined for the cell wall. The first step in mannan synthesis is the initiation and extension of an ␣-1,6-linked polymannose backbone. This requires the sequential action of two enzyme complexes, mannan polymerases (M-Pol) I and II. M-Pol I contains the proteins Mnn9p and Van1p, although the stoichiometry and individual contributions to enzyme action are unclear. We report here that the two proteins are each present as a single copy in the complex. Both proteins contain a DXD motif found in the active site of many glycosyltransferases, and mutations in this motif in Mnn9p or Van1p reveal that both proteins contribute to mannose polymerization. However, the effects of these mutations on both the in vivo and in vitro activity are distinct, suggesting that the two proteins may have different roles in the complex. Finally, we show that a simple glycoprotein based on hen egg lysozyme can be used as a substrate for modification by purified M-Pol I in vitro.

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Genes and Enzymes of theGT31Family: Towards Unravelling The Function(s) of the Plant Glycosyltransferase Family Members

Egelund

Ellis

Doblin

et al. 2018

Annual Plant Reviews Online

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The galactosyltransferases (GalTs) have been extensively studied in mammals where they are involved in the synthesis of bothN‐ andO‐glycans on glycoproteins. In contrast, only a few studies have been published characterizing plant GalTs even though plants assemble many complex carbohydrates and glycoconjugates not found in other eukaryotes or bacteria, such as pectins, galactomannans, xyloglucans, arabinogalactan‐proteins (AGPs), proline‐rich proteins and extensins. Many enzymes characterized within family GT31 are mammalian and include the fringe proteins (GlcNAc‐β‐(1,3)‐Fuc), the chondroitin synthases (GlcUA‐β‐(1,3)‐GalNAc), and the β‐(1,3)‐GalTs. We attempted to categorize the putative β‐(1,3)‐GalTs and, where possible, we predicted their putative substrate specificity based on secondary structure and motifs shared with known β‐(1,3)‐GalTs. Ninety‐four plant sequences are assigned to CAZy family GT31, including 33 fromArabidopsis thaliana(At), and 39 fromOryza sativa(Os), but only one plant enzyme has as yet been biochemically characterized, At‐GalT1, which is involved in the production of the Lewisastructure ofN‐glycans (Gal β‐(1,3)‐GlcNAc). Phylogenetic analysis identified 11 distinct clades, of which 4 are plant‐specific. Clade 1 proteins contain the plant‐specific DUF604 domain. Clade 7 is defined by a galectin‐containing domain and both clades 7 and 10 contain GalT domains. The possible substrate specificity of these enzymes is predicted. Clade 11 proteins contain no obvious domains so no function can be assigned. Enzymes in clades 7 and 10 are speculated to be involved in the synthesis of both proteoglycans, such as AGPs, andN‐glycans.

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The Notch signalling regulator Fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DxD

Abstract: These results indicate that Fringe does not exert its effects outside of the cell, but rather acts in the Golgi apparatus, apparently as a glycosyltransferase. They suggest that alteration in receptor glycosylation can regulate the relative efficiency of different ligands.

Cited by 179 publications

References 48 publications

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

Biogenesis of Golgi Stacks in Imaginal Discs ofDrosophila melanogaster

The Components of the Saccharomyces cerevisiaeMannosyltransferase Complex M-Pol I Have Distinct Functions in Mannan Synthesis

Genes and Enzymes of theGT31Family: Towards Unravelling The Function(s) of the Plant Glycosyltransferase Family Members

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