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Glycans in evolution and development. Workshop on glycoscience and development - PubMed

Glycans in evolution and development. Workshop on glycoscience and development

Catherine L R Merry et al. EMBO Rep. 2008 Jul.

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Figures

Figure 1
Figure 1

Properties of O-linked N-acetylglucosamine (O-GlcNAc) as described by G. Hart (Baltimore, MD, USA). O-GlcNAc is a dynamic post-translational modification of nuclear and cytoplasmic proteins. Cycling of O-GlcNAc is regulated by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase. Between 2% and 5% of glucose is metabolized to O-GlcNAc from UDP-GlcNAc, which is the donor for GlcNAcylation. GlcNAcylation is sensitive to nutrients and to cellular stress, and seems to be important in signalling, transcription and human diseases (including diabetes and neurodegenerative disorders). The inset represents a western blot of a two-dimensional gel of nuclear and cytoplasmic proteins from the human HeLa cell line, probed with an antibody against O-GlcNAc, which illustrates the large number of proteins that are modified by O-GlcNAc.

Figure 2
Figure 2

Structure of α-dystroglycan as described by J. Hewitt (Nottingham, UK). Diagrammatic structure of the α-dystroglycan molecule showing its different regions and functional activities. The glycans under discussion are linked to the peptide in the mucin-like SEA (sea urchin sperm protein, enterokinase and agrin) extracellular domain of the molecule. O-GlcNAc, N-acetylglucosamine; OGT, O-GlcNAc transferase.

Figure 3
Figure 3

Evolution of fucosyltransferases as described by R. Oriol (Paris, France). Phylogenetic tree of α2-FUTs, α6-FUTs and protein-O-FUTs (POFUTs) illustrating the common origin (red triangle, at the root of the tree), the two duplications at the origin of the α2/6-FUT and the POFUT1/2 branches (red circles), and the two duplications at the origin of the three families of vertebrate α2-FUTs (red squares). The yellow circle shows the position of a retro-transposition event, which occurred in the vertebrate branch of α2-FUT and induced the loss of all the introns in the coding sequences of these genes, which are therefore monoexonic. FUT, fucosyltransferase; Sec1, Secretor locus-encoded α(1,2)fucosyltransferase 1.

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Catherine L.R. Merry

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Sviatlana A. Astrautsova

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This EMBO Workshop on Glycoscience and Development took place between 9 and 12 December, 2007, in Lille, France, and was organized by P. Delannoy, Y. Guérardel, T. Merry and J.-C. Michalski.

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