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Taylor & Drickamer: Introduction to Glycobiology: 2e

Chapter 09

Key References:

Braakman, I. (2001) A novel lectin in the secretory pathway: an elegant mechanism for glycoprotein elimination. EMBO Reports 2, 666–668. This is a short review of the evidence for involvement of a mannosidase-type lectin in degradation of misfolded proteins.
http://www.nature.com/embor/journal/v2/n8/pdf/embor358.pdf

Dagher, S. F., Wang, J. L., and Patterson, R. J. (1995) Identification of galectin-3 as a factor in pre-mRNA splicing. Proceedings of the National Academy of Sciences USA 92, 1213–1217. This paper, and Park et al. (2001, see below), present evidence for the involvement of galectins in RNA splicing.
http://www.pnas.org/cgi/reprint/92/4/1213.pdf

Dahms , N.M. and Hancock, M.K. (2002) P-type lectins. Biochimica et Biophysica Acta 1572 , 317-340. A detailed review of the structure and functions of the mannose 6-phosphate receptors.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T1W-4683X99-6-7&_cdi=4901&_user=217827&_orig=search&_coverDate=09%2F19%2F2002&_qd=1&_sk=984279997&view=c&wchp=dGLbVzz-zSkzV&md5=f67d0334eb7ffcb539cc99207db3ee85&ie=/sdarticle.pdf]

Fiete, D. J., Beranek, M. C., and Baenziger, J. U. (1998) A cysteine-rich domain of the ‘mannose’ receptor mediates GalNAc-4-SO 4 binding. Proceedings of the National Academy of Sciences USA 95, 2089–2093. Experiments showing that the R-type CRD of the mannose receptor binds to the sulphated sugars on glycoprotein hormones are described.
http://www.pnas.org/cgi/reprint/95/5/2089.pdf

Hauri, H.-P., Appenzeller, C., Kuhn, F., and Nufer, O. (2000) Lectins and traffic in the secretory pathway. FEBS Letters 476, 32–37. The functions of ERGIC-53 are reviewed.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-40K8V61-8-5&_cdi=4938&_user=217827&_orig=search&_coverDate=06%2F30%2F2000&_qd=1&_sk=995239998&view=c&wchp=dGLbVlb-zSkWz&md5=39de06cf1de5f105003920d6885a80e6&ie=/sdarticle.pdf]

Helenius, A. and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science 291, 2364–2369. This review, and Helenius and Aebi (2004, see below) provide details of the roles of glycans and proteins that recognise them in glycoprotein folding quality control and transport. quality control and transport.
[Your institution will need to be a subscriber to access this article online at: http://www.sciencemag.org/cgi/reprint/291/5512/2364.pdf]

Helenius, A. and Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annual Review of Biochemistry 73 , 1019-1049.
http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.biochem.73.011303.073752

Kolatkar, A.R., Leung, A.K., Isecke, R., Brossmer, R., Drickamer, K., and Weis, W.I. (1998) Mechanism of N-acetylgalactosamine binding to a C-type animal lectin carbohydrate-recognition domain. Journal of Biological Chemistry 273, 19502–19508. The structural basis for selective binding of GalNAc and galactose to a C-type CRD, such as that of the asialoglycoprotein receptor is described.
http://www.jbc.org/cgi/reprint/273/31/19502.pdf

Lee, S. J., Evers, S., Roeder, D., Parlow, A. F., Risteli, J., Risteli, L., Lee, Y. C., Feizi, T., Langen, H., and Nussenzweig, M. C. (2002) Mannose receptor-mediated regulation of serum glycoprotein homeostasis. Science 295, 1898–1901. This paper presents analysis of the mannose receptor knockout mouse, providing evidence for the receptor’s role in glycoprotein clearance.
[Your institution will need to be a subscriber to access this article online at: http://www.sciencemag.org/cgi/reprint/295/5561/1898.pdf]

Lord, M.J. and Frigerio, L. (2002) ER quality control: A function for sugars in the cytosol. Current Biology 12, 162-164. A short commentary describing the role of sugar-binding F-box proteins in endoplasmic reticulum-associated protein degradation.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRT-46X26XT-C-3&_cdi=6243&_user=217827&_orig=search&_coverDate=10%2F01%2F2002&_qd=1&_sk=999879980&view=c&wchp=dGLbVtb-zSkzV&md5=4de88ce90d97e31f31ed0423e3d72e14&ie=/sdarticle.pdf]

Park, J. W., Voss, P. G., Grabski, S., Wang, J. L., and Patterson, R. J. (2001) Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein. Nucleic Acids Research 29, 3595–3602.
http://nar.oxfordjournals.org/cgi/reprint/29/17/3595.pdf

Rice, K. G., Weisz, O. A., Barthel, T., Lee, R. T., and Lee, Y. C. (1990) Defined stoichiometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat hepatocytes. Journal of Biological Chemistry 265, 18429–18434. Experiments demonstrating the importance of oligosaccharide geometry for high affinity binding to the asialoglycoprotein receptor are described.
http://www.jbc.org/cgi/reprint/265/30/18429.pdf

Roberts, D.L., Weix, D.J., Dahms, N.M., and Kim, J.-J.P. (1998) Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell 93, 639–648. The crystal structure of a P-type CRD is described.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-4194SH6-J-N&_cdi=7051&_user=217827&_orig=search&_coverDate=05%2F15%2F1998&_qd=1&_sk=999069995&view=c&wchp=dGLbVzb-zSkWz&md5=c9829c919c2e188a3f53dc5e0114974c&ie=/sdarticle.pdf

Schrag, J. D., Bergeron, J. J. M., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., and Cygler, M. (2001) The structure of calnexin, an ER chaperone involved in quality control of protein folding. Molecular Cell 8, 633–644. The crystal structure of calnexin is described, giving insights into the mechanism of oligosaccharide binding.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSR-4448RPS-M-Y&_cdi=7053&_user=217827&_orig=search&_coverDate=09%2F30%2F2001&_qd=1&_sk=999919996&view=c&wchp=dGLbVtz-zSkWb&md5=fbb7cec732c7844f9ebde80c790710d5&ie=/sdarticle.pdf

Spiess, M. (1990) The asialoglycoprotein receptor: a model for endocytic transport receptors. Biochemistry 29, 10008–10019. The function of the asialoglycoprotein receptor in endocytosis is reviewed in detail.
http://pubs.acs.org/cgi-bin/archive.cgi/bichaw/1990/29/i43/pdf/bi00495a001.pdf

Tozawa, R., Ishibashi, S., Osuga, J., Yamamoto, K., Yagyu, H., Ohashi, K., Tamura, Y., Yahagi, N., Iizuka, Y., Okazaki, H., Harada, K., Gotoda, T., Shimano, H., Kimura, S., Nagai, R., and Yamada, N. (2001) Asialoglycoprotein receptor deficiency in mice lacking the major receptor subunit: its obligate requirement for the stable expression of oligomeric receptor. Journal of Biological Chemistry 276, 12624–12628. Analysis of glycoprotein clearance in the asialoglycoprotein receptor knockout mouse is presented.
http://www.jbc.org/cgi/reprint/276/16/12624.pdf

Questions

4) Describe how the mannose 6-phosphate binding sites in the cation-independent mannose 6-phosphate receptor have been characterized.

References:

Hancock, M.K., Yammani, R.D. and Dahms N.M. (2002) Localization of the carbohydrate recognition sites of the insulin-like growth factor II/mannose 6-phosphate receptor to domains 3 and 9 of the extracytoplasmic region. Journal of Biological Chemistry 277, 47205-47212.
http://www.jbc.org/cgi/reprint/277/49/47205.pdf

Hancock, M.K., Haskins, D.J., Sun, G. and Dahms, N.M. (2002) Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor. Journal of Biological Chemistry 277, 11255-11264.
http://www.jbc.org/cgi/reprint/277/13/11255.pdf

Westlund, B., Dahms, N.M. and Kornfeld, S. (1991) The bovine mannose 6-phosphate/insulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region. Journal of Biological Chemistry 266, 23233-23239.
http://www.jbc.org/cgi/reprint/266/34/23233.pdf

5) Discuss the experimental and medical evidence that ERGIC-53 is needed to transport some glycoproteins out of the endoplasmic reticulum.

References:

Appenzeller, C., Andersson, H., Kappeler, F. and Hauri H.-P. (1999) The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nature Cell Biology 1, 330-334.
[You must have a username and password to access the full article at http://www.nature.com/ncb/journal/v1/n6/pdf/ncb1099_330.pdf]

Moussali, M., Pipe, S.W., Hauri, H.P., Nichols, W.C., Ginsburg, D. and Kaufman, R.J. (1999) Mannose-dependent ERGIC-53-mediated ER to Golgi trafficking of coagulation factors V and VIII. Journal of Biological Chemistry 274, 32539-32542.
http://www.jbc.org/cgi/reprint/274/46/32539.pdf

Nichols, W.C., Seligsohn, U., Zivelin, A., Terry, V.H., Hertel, C.E., Wheatley, M.A., Moussali, M.J., Hauri, H.-P., Ciavarella, N., Kaufman, R.J. and Ginsburg, D. (1998) Mutations in the gene for ERGIC-53, a protein of the endoplasmic reticulum-Golgi intermediate compartment, cause combined deficiency of coagulation factors V and VIII. Cell 93, 61-70.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-419K1G5-B-G&_cdi=7051&_user=217827&_orig=search&_coverDate=04%2F03%2F1998&_qd=1&_sk=999069998&view=c&wchp=dGLzVlz-zSkzS&md5=e296a5e097e5f03c0e30bb18707631e9&ie=/sdarticle.pdf]

6) Discuss how experiments with knockout mice have provided strong evidence that the mannose receptor clears mannose-terminated glycoproteins from the circulation, but have cast doubt on a role for the asialoglycoprotein receptor in clearance of desialylated glycoproteins. Refer to the papers by Lee et al. (2002)
http://www.sciencemag.org/cgi/reprint/295/5561/1898.pdf and Tozawa et al. (2001) http://www.jbc.org/cgi/reprint/276/16/12624.pdf in the reference list.

Box 9.1 Glycotherapeutics: Glycosylation of recombinant glycoproteins must be carefully controlled
Lead references:

Elliott, S., Lorenzini, T., Asher, S., Aoki, K., Brankow, D., Buck, L., Busse, L., Chang, D., Fuller, J., Grant, J., Hernday, N., Hokum, M., Hu, S., Knudten, A., Levin, N., Komorowski, R., Martin, F., Navarro, R., Osslund, T., Rogers, G., Rogers, N., Trail, G. and Egrie, J. (2003) Enhancement of therapeutic protein activities through glycoengineering. Nature Biotechnology 21, 414-421.
http://www.nature.com/nbt/journal/v21/n4/pdf/nbt799.pdf

Elliott, S., Egrie, J., Browne, J., Lorenzini, T., Busse, L., Rogers, N. and Ponting, I. (2004) Control of rHuEPO biological activity: The role of carbohydrate. Experimental Hematology 32, 1146-1155.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VP8-4F0096J-4-1&_cdi=6200&_user=217827&_orig=search&_coverDate=12%2F01%2F2004&_qd=1&_sk=999679987&view=c&wchp=dGLbVlz-zSkWb&md5=78fcbac40a6929c8bea8ca121969f1b9&ie=/sdarticle.pdf]

Takeuchi, M., Takasaki, S., Miyazaki, H., Kato, T., Hoshi, S., Kochibe, N. and Kobata, A. (1988) Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. Journal of Biological Chemistry 263, 3657-3663.
http://www.jbc.org/cgi/reprint/263/8/3657.pdf