Taylor & Drickamer: Introduction to Glycobiology: 2e 
Key Reading References
Answers to ProblemsTaylor & Drickamer: Introduction to Glycobiology: 2e
Chapter 04
Key References
Fundernurgh, J.L. (2000) Keratan sulfate: structure, biosynthesis, and function. Glycobiology 10, 951–958. The biochemistry and biology of keratan sulphate are reviewed in detail.
http://glycob.oxfordjournals.org/cgi/reprint/10/10/951.pdf
Hanisch, F.-G., Reis, C.A., Clausen, H., and Paulsen, H. (2001) Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides. Glycobiology 11, 731–740. Experiments demonstrating specific substrate requirements for O-glycosylation by GalNAc-transferases are presented.
http://glycob.oxfordjournals.org/cgi/reprint/11/9/731.pdf
Heikkinen, J., Risteli, M., Wang, C., Latvala, J., Rossi, M., Valtavaara, M., and Myllyla, R. (2000) Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. Journal of Biological Chemistry 275, 36158–36163. Characterization of the enzyme that hydroxylates and glucosylates lysine residues in collagen is presented.
http://www.jbc.org/cgi/reprint/275/46/36158.pdf
Kim, Y.S., Gum, J., Jr., and Brockhausen, I. (1996) Mucin glycoproteins in neoplasia. Glycoconjugate Journal 13, 693–707. Changes in expression and structure of mucins in cancer are discussed.
http://www.springerlink.com/media/d48072xvrlckyntkuw1h/contributions/v/7/2/2/v722385015802534.pdf
Marth, J.D. (1996) Complexity of O-linked oligosaccharide biosynthesis engendered by multiple polypeptide N-acetylgalactosaminyltransferases. Glycobiology 6, 701–705. This is a short review discussing the potential roles of different GalNAc-transferases in biosynthesis of O-linked oligosaccharides. Not available online.
Perez-Villar, J. and Hill, R.L. (1999) The structure and assembly of secreted mucins. Journal of Biological Chemistry 274, 31751–31754. This is a short but detailed review of the biochemistry of mucins.
http://www.jbc.org/cgi/reprint/274/45/31751.pdf
van den Steen, P., Rudd, P.M., Dwek, R.A., and Opdenakker, G. (1998) Concepts and principles of O-linked glycosylation. Critical Reviews in Biochemistry and Molecular Biology 33, 151–208. The structures, biosynthesis, and functions of different types of O-linked glycans are reviewed. Not available online.
Vertel, B.M. (1995) The ins and outs of aggrecan. Trends in Cell Biology 5, 458–464. The biology and biochemistry of the proteoglycan aggrecan are reviewed.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6TCX-40W0VBP-6V-1&_cdi=5182&_user=217827&_orig=browse&_coverDate=12%2F31%2F1995&_sk=999949987&view=c&wchp=dGLbVlz-zSkzk&md5=6fba3f1b64e3b16259e712fcc9b23a22&ie=/sdarticle.pdf]
Vestweber, D. and Blanks, J.E. (1999) Mechanisms that regulate the function of selectins and their ligands. Physiological Reviews 79, 181–213. The structures and functions of the selectins and their glycoprotein ligands are reviewed in detail.
http://physrev.physiology.org/cgi/reprint/79/1/181.pdf
Zachara, N.E. and Hart, G.W. (2004a) O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochimica et Biophysica Acta 1673, 13-28. A detailed review of the evidence for the roles of O-GlcNAc as a dynamic modification of nuclear and cytoplasmic proteins.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T1W-4CBHTCR-1-C&_cdi=4901&_user=217827&_orig=search&_coverDate=07%2F06%2F2004&_qd=1&_sk=983269998&view=c&wchp=dGLbVtb-zSkWb&md5=1608b72699f30a99e775c6e412d20fa8&ie=/sdarticle.pdf]
Zachara, N.E. and Hart, G.W. (2004b) O-GlcNAc modification: A nutritional sensor that modulates proteasome function. Trends in Cell Biology14, 218-221. A short review of the evidence that O-GlcNAc modification controls activity of the proteasome.
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Questions
4) Why is it difficult to predict sites of O-linked glycosylation from examination of the amino acid sequences of proteins? What can be learned from comparison of sequences of proteins known to have O-linked glycosylation sites?
Reference: Hema Thanka Christlet, T. and Veluraja, K. (2001) Database analysis of O-glycosylation sites in proteins. Biophysical Journal 80, 952-960.
http://www.biophysj.org/cgi/reprint/80/2/952.pdf
6) Assess the evidence that addition of O-linked fucose to proteins occurs in the endoplasmic reticulum rather than in the Golgi.
Reference: Luo, Y. and Haltiwanger, R.S. (2005) O-fucosylation of notch occurs in the endoplasmic reticulum. Journal of Biological Chemistry 280, 11289-11294.
http://www.jbc.org/cgi/reprint/280/12/11289.pdf
Box 4.1 Glycobiology of disease: Changes in O-linked GlcNAc are linked to Alzheimer's disease
Lead references:
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G.W. and Gong, C.-X. (2004) O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease. Proceedings of the National Academy of Sciences USA 101, 10804-10809.
http://www.pnas.org/cgi/reprint/101/29/10804.pdf
Lefebvre, T., Ferreira, S., Dupont-Wallois, L., Bussière, T., Dupire, M.-J., Delacourte, A., Michalski, J.-C., Caillet-Boudin, M.-L. (2002) Evidence of a balance between phosphorylation and O-GlcNAc glycosylation of Tau proteins - a role in nuclear localization. Biochimica et Biophysica Acta 1619, 167-176.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T1W-473VSBK-3-F&_cdi=4901&_user=217827&_orig=search&_coverDate=01%2F20%2F2003&_qd=1&_sk=983809997&view=c&wchp=dGLzVzz-zSkzS&md5=a511759cc64b669f0022e18481ccc614&ie=/sdarticle.pdf]
Arnold, C.S., Johnson, G.V.W., Cole, R.N., Dong, D. L.-Y., Lee, M. and Hart, G.W. (1996) The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. Journal of Biological Chemistry 271, 28741-28744.
http://www.jbc.org/cgi/reprint/271/46/28741.pdf
Yao, P.J. and Coleman, P.D. (1998) Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease. The Journal of Neuroscience 18, 2399-2411.
http://www.jneurosci.org/cgi/reprint/18/7/2399.pdf
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