Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor

Cell

Volumn 93, Issue 4, 1998, Pages 639-648

  Roberts, David L ^a   Weix, Daniel J ^a   Dahms, Nancy M ^a   Kim, Jung Ja P ^a  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID HYDROLASE; AVIDIN; BETA GLUCURONIDASE; CARBOHYDRATE; CATION DEPENDENT MANNOSE 6 PHOSPHATE RECEPTOR; DIMER; LYSOSOME ENZYME; SOMATOMEDIN B; SOMATOMEDIN B RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; GLYCOSYLATION; LYSOSOME; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; RECEPTOR AFFINITY; SEQUENCE HOMOLOGY; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION;

ANIMALIA; BOVINAE;

EID: 0032524316     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81192-7     Document Type: Article

References (50)

1. Brünger, A.T. (1992). X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR. (New Haven, CT: Yale University Press).
2. Carter, C., and Carter, C. (1979). Protein crystallization using incomplete factorial experiments. J. Biol. Chem. 246, 12219-12223.
3. Dahms, N.M., and Brzycki-Wessell, M.A. (1995). Expression and characterization of functional bovine cation-dependent mannose 6-phosphate receptors in baculovirus-infected insect cells. Arch. Biochem. Biophys. 317, 497-503.
4. Dahms, N.M., and Kornfeld, S. (1989). The cation-dependent mannose 6-phosphate receptor: structural requirements for mannose 6-phosphate binding and oligomerization. J. Biol. Chem. 264, 11458-11467.
5. Dahms, N.M., Lobel, P., Breitmeyer, J., Chirgwin, J.M., and Kornfeld, S. (1987). 46 kDa mannose 6-phosphate receptor: cloning, expression, and homology to the 215 kDa mannose 6-phosphate receptor. Cell 50, 181-192.
6. Dahms, N.M., Lobel, P., and Kornfeld, S. (1989). Mannose 6-phosphate receptors and lysosomal enzyme targeting. J. Biol. Chem. 264, 12115-12118.
7. Dahms, N.M., Rose, P.A., Molkentin, J.D., Zhang, Y., and Brzycki, M.A. (1993). The bovine mannose 6-phosphate/insulin-like growth factor II receptor. The role of arginine residues in mannose 6-phosphate binding. J. Biol. Chem. 268, 5457-5463.
8. Distler, J.J., Guo, J., Jourdian, G.W., Srivastava, O.P., and Hindsgaul, O. (1991). The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides. J. Biol. Chem. 266, 21687-21692.
9. Drickamer, K. (1995). Multiplicity of lectin-carbohydrate interactions. Nat. Struct. Biol. 2, 437-439.
10. Drickamer, K., and Taylor, M.E. (1993). Biology of animal lectins. Annu. Rev. Cell Biol. 9, 237-264.
11. Furey, W., and Swaminathan, S. (1997). PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. In Macromolecular Crystallography Methods in Enzymology, C. Carter and R. Sweet, eds. (Orlando, FL: Academic Press).
12. 1 macrophage membranes lacking the 215-kDa mannose 6-phosphate receptor: evidence for the existence of a second mannose 6-phosphate receptor. Proc. Natl. Acad. Sci. USA 82, 4428-4432.
13. Hoflack, B., and Kornfeld, S. (1985b). Purification and characterization of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver. J. Biol. Chem. 260, 12008-12014.
14. Hoflack, B., Fujimoto, K., and Kornfeld, S. (1987). The interaction of phosphorylated oligosaccharides and lysosomal enzymes with bovine liver cation-dependent mannose 6-phosphate receptor. J. Biol. Chem. 262, 123-129.
15. Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
16. Jain, S., Drendel, W.B., Chen, Z.-W., Mathews, F.S., Sly, W.S., and Grubb, J.H. (1996). Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat. Struct. Biol. 3, 375-381.
17. Kornfeld, S. (1992). Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Annu. Rev. Biochem. 61, 307-330.
18. Köster, A., Nagel, G., von Figura, K., and Pohlmann, R. (1991). Molecular cloning of the mouse 46-kDa mannose 6-phosphate receptor (MPR46). Biol. Chem. 372, 297-300.
19. Li, M., Distler, J.J., and Jourdian, G.W. (1990). The aggregation and dissociation properties of a low molecular weight mannose 6-phosphate receptor from bovine testis. Arch. Biochem. Biophys. 283, 150-157.
20. Livnah, O., Bayer, E.A., Wilchek, M., and Sussman, J.L. (1993). Three-dimensional structures of avidin and the avidin-biotin complex. Proc. Natl. Acad. Sci. USA 90, 5076-5080.
21. Lobel, P., Dahms, N.M., and Kornfeld, S. (1988). Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. J. Biol. Chem. 263, 2563-2570.
22. Ma, Z., Grubb, J.H., and Sly, W.S. (1991). Cloning, sequencing, and functional characterization of the murine 46-kDa mannose 6-phosphate receptor. J. Biol. Chem. 266, 10589-10595.
23. Ma, Z., Grubb, J.H., and Sly, W.S. (1992). Divalent cation-dependent stimulation of ligand binding to the 46-kDa mannose 6-phosphate receptor correlates with divalent cation-dependent tetramerization. J. Biol. Chem. 267, 19017-19022.
24. Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 3, 491-497.
25. McPherson, A. (1982). Preparation and Analysis of Protein Crystals. (New York: Wiley).
26. Munier-Lehmann, H., Mauxion, F., and Hoflack, B. (1996a). Function of the two mannose 6-phosphate receptors in lysosomal enzyme transport. Biochem. Soc. Trans. 24, 133-136.
27. Munier-Lehmann, H., Mauxion, F., Bauer, U., Lobel, P., and Hoflack, B. (1996b). Re-expression of the mannose 6-phosphate receptors in receptor-deficient fibroblasts. Complementary function of the two mannose 6-phosphate receptors in lysosomal enzyme targeting. J. Biol. Chem. 271, 15166-15174.
28. Neufeld, E.F. (1991). Lysosomal storage diseases. Annu. Rev. Biochem. 60, 257-280.
29. Otowinski, Z., and Minor, W. (1996). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
30. Punnonen, E.-L., Wilke, T., von Figura, K., and Hille-Rehfeld, A. (1996). The oligomeric state of 46-kDa mannose 6-phosphate receptor does not change upon intracellular recycling and binding of ligands. Eur. J. Biochem. 237, 809-818.
31. Read, R.A. (1986). Improved coefficients for map calculation using partial structures with errors. Acta Crystallogr. D5, 760-763.
32. Roussel, A., and Cambillau, C. (1994). TURBO-FRODO, the Manual (Version 4.2). (Marseille, France: Biographics, LCCMB).
33. Shipley, J.M., Grubb, J.H., and Sly, W.S. (1993). The role of glycosylation and phosphorylation in the expression of active human β-glucuronidase. J. Biol. Chem. 268, 12193-12198.
34. Sleat, D.E., and Lobel, P. (1997). Ligand binding specificities of the two mannose 6-phosphate receptors. J. Biol. Chem. 272, 731-738.
35. Stein, M., Meyer, H.E., Hasilik, A., and von Figura, K. (1987). 46-kDa mannose 6-phosphate-specific receptor: purification, subunit composition, chemical modification. Biol. Chem. 368, 927-936.
36. Terwilliger, T. (1994). HEAVY (Version 3.0) Manual. (Los Alamos, NM: Los Alamos National Laboratories).
37. Tong, P.Y., and Kornfeld, S. (1989). Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor. J. Biol. Chem. 264, 7970-7975.
38. Tong, P.Y., Tollefsen, S.E., and Kornfeld, S. (1988). The cation-independent mannose 6-phosphate receptor binds insulin-like growth factor II. J. Biol. Chem. 263, 2585-2588.
39. Tong, P.Y., Gregory, W., and Kornfeld, S. (1989). Ligand interactions of the cation-independent mannose 6-phosphate receptor. The stoichiometry of mannose 6-phosphate binding. J. Biol. Chem. 264, 7962-7969.
40. von Figura, K., and Hasilik, A. (1986). Lysosomal enzymes and their receptors. Annu. Rev. Biochem. 55, 167-193.
41. Waheed, A., Braulke, T., Junghans, U., and von Figura, K. (1988). Mannose 6-phosphate/insulin like growth factor II receptor: the two types of ligand bind simultaneously to one receptor at different sites. Biochem. Biophys. Res. Commun. 152, 1248-1254.
42. Waheed, A., Hille, A., Junghans, U., and von Figura, K. (1990). Quaternary structure of the Mr 46,000 mannose 6-phosphate specific receptor: effect of ligand, pH, and receptor concentration on the equilibrium between dimeric and tetrameric receptor forms. Biochemistry 29, 2449-2455.
43. Wang, B.C. (1985). Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112.
44. Watanabe, H., Grubb, J.H., and Sly, W.S. (1990). The overexpressed human 46-kDa mannose 6-phosphate receptor mediates endocytosis and sorting of β-glucuronidase. Proc. Natl. Acad. Sci. USA 87, 8036-8040.
45. Weis, W.I., and Drickamer, K. (1996). Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem. 65, 441-473.
46. Wendland, M., Hille, A., Nagel, G., Waheed, A., von Figura, K., and Pohlmann, R. (1989). Synthesis of a truncated Mr 46000 mannose 6-phosphate receptor that is secreted and retains ligand binding. Biochem. J. 260, 201-206.
47. Wendland, M., Waheed, A., von Figura, K., and Pohlmann, R. (1991 a). Mr 46,000 mannose 6-phosphate receptor. The role of histidine and arginine residues for binding of ligands. J. Biol. Chem. 266, 2917-2923.
48. Wendland, M., von Figura, K., and Pohlmann, R. (1991b). Mutational analysis of disulfide bridges in the Mr 46,000 mannose 6-phosphate receptor. Localization and role for ligand binding. J. Biol. Chem. 266, 7132-7136.
49. 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. J. Biol. Chem. 266, 23233-23239.
50. Zhang, Y., and Dahms, N.M. (1993). Site-directed removal of N-glycosylation sites in the bovine cation-dependent mannose 6-phosphate receptor: effects on ligand binding, intracellular targeting and association with binding immunoglobulin protein. Biochem. J. 295, 841-848.