Hemophilic adhesion by cadherins

Current Opinion in Structural Biology

Volumn 9, Issue 2, 1999, Pages 275-281

  Koch, Alexander W ^a,b   Bozic, Damir ^a   Pertz, Olivier ^a   Engel, Jürgen ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN;

CELL ADHESION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; REVIEW; AMINO ACID SUBSTITUTION; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON MICROSCOPY; MACROMOLECULE; PHYSIOLOGY; PROTEIN CONFORMATION; STEREOISOMERISM; ULTRASTRUCTURE;

AMINO ACID SUBSTITUTION; ANIMALS; CADHERINS; CELL ADHESION; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PROTEIN CONFORMATION; STEREOISOMERISM;

EID: 0033106491     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80038-4     Document Type: Article

References (41)

1. Takeichi M: Morphogenic roles of classical cadherins. Curr Opin Cell Biol 1995, 7:619-627.
2. Gumbiner BM: Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell 1996, 84:345-357.
3. Redies C: Cadherins and the formation of neural circuitry in the vertebrate CNS. Cell Tissue Res 1997, 290:405-413.
4. Fannon AM, Colman DR: A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins. Neuron 1996, 17:423-434.
5. Benson DL, Tanaka H: N-cadherin redistribution during synaptogenesis in hippocampal neurons. J Neurosci 1998, 18:6892-6904. This works once again illustrates the presence of classic cadherins in central nervous system synapses (see, also, [4,33•]) and suggests that cadherins are involved in defining the specificity of developing synapses.
6. Mareel M, Boterberg T, Noe V, Van Hoorde L, Vermeulen S, Bruyneel E, Bracke M: E-cadherin/catenin/cytoskeleton complex: A regulator of cancer invasion. J Cell Physiol 1997, 173:271-274.
7. Perl AK, Wilgenbus P, Dahl U, Semb H, Christofori G: A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature 1998, 392:190-193. In this important paper, a transgenic mouse model was used to demonstrate that the loss of E-cadherin is a crucial step in the transition from benign to invasive tumors.
8. Marra A, Isberg RR: Bacterial pathogenesis: Common entry mechanisms. Curr Biol 1996, 6:1084-1086.
9. Suzuki ST: Protocadherins and diversity of the cadherin superfamily. J Cell Sci 1996, 109:2609-2611.
10. 2+-dependent cell adhesion molecule. Bioessays 1989, 11:88-91.
11. Barth AI, Nathke IS, Nelson WJ: Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways. Curr Opin Cell Biol 1997, 9:683-690. A comprehensive review describing the connection between members of the cadherin-catenin complex and signaling pathways.
12. Aberle H, Schwarte H, Kemler R: Cadherin-catenin complex: Protein interactions and their implications for cadherin function. J Cell Biochem 1996, 61:514-523.
13. Hyafil F, Babinet C, Jacob F: Cell-cell interactions in early embryogenesis: A molecular approach to the role of calcium. Cell 1981, 26:447-454.
14. Takeichi M: Cadherins: A molecular family important in selective cell-cell adhesion. Annu Rev Biochem 1990, 59:237-252.
15. Nose A, Tsuji K, Takeichi M: Localization of specificity determining sites in cadherin cell adhesion molecules. Cell 1990, 61:147-155.
16. Overduin M, Harvey TS, Bagby S, Tong KI, Yau P, Takeichi M, Ikura M: Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science 1995, 267:386-389.
17. Shapiro L, Fannon AM, Kwong PD, Thompson A, Lehmann MS, Grubel G, Legrand JF, Als-Nielsen J, Colman DR, Hendrickson WA: Structural basis of cell-cell adhesion by cadherins. Nature 1995, 374:327-337.
18. Nagar B, Overduin M, Ikura M, Rini JM: Structural basis of calcium- Induced E-cadherin rigidification and dimerization. Nature 1996, 380:360-364.
19. Pokutta S, Herrenknecht K, Kemler R, Engel J: Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding. Eur J Biochem 1994, 223:1019-1026.
20. 2+ binding site of uvomorulin abolish the adhesive function. Cell 1990, 63:1033-1038.
21. Alattia JR, Ames JB, Porumb T, Tong KI, Heng YM, Ottensmeyer P, Kay CM, Ikura M: Lateral self-assembly of E-cadherin directed by cooperative calcium binding. FEBS Lett 1997, 417:405-408.
22. Koch AW, Pokutta S, Lustig A, Engel J: Calcium binding and homoassociation of E-cadherin domains. Biochemistry 1997, 36:7697-7705. The authors present the first equilibrium dissociation constants for calcium binding to a cadherin. Binding data were evaluated for the most N-terminal binding pocket and for the entire ectodomain (comprising four binding pockets). Surprisingly, the most N-terminal pocket harbors much weaker binding sites and it was conjectured that calcium binding to this pocket might be implicated in homophilic interactions - a hypothesis that was later supported by the work of Pertz et al. [30•].
23. Tomschy A, Fauser C, Landwehr R, Engel J: Homophilic adhesion of E-cadherin occurs by a co-operative two-step interaction of N- Terminal domains. EMBO J 1996, 15:3507-3514.
24. Vestweber D, Gossler A, Boller K, Kemler R: Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos. Dev Biol 1987, 124:451-456.
25. Boller K, Vestweber D, Kemler R: Cell-adhesion molecule uvomorulin is localized in the intermediate junctions of adult intestinal epithelial cells. J Cell Biol 1985, 100:327-332.
26. Adams CL, Chen YT, Smith SJ, Nelson WJ: Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein. J Cell Biol 1998, 142:1105-1119. This paper describes the application of a fully functional E-cadherin-GFP fusion protein to distinguish between three consecutive stages in cell-cell adhesion. The authors present a model of how initial weak adhesion is transformed into strong adhesion by concerted reorganization of E-cadherin molecules and the actin cytoskeleton.
27. Yap AS, Brieher WM, Pruschy M, Gumbiner BM: Lateral clustering of the adhesive ectodomain: A fundamental determinant of cadherin function. Curr Biol 1997, 7:308-315. In this study, an elegant method was used to cluster C-cadherin ectodomains on the cell surface independently of cytoskeletal interactions. The cytosolic domain of C-cadherin was replaced by several FK-binding protein (FKBP, see [37]) domains. Adding the organic compound FK1012, which can easily diffuse through the cell membrane, leads to the dimerization of FKBP domains and, therefore, to the clustering of C-cadherin extracellular domains. The clustered cadherin mediated cell adhesion in the absence of cytoskeletal interactions.
28. Takeda H, Nagafuchi A, Shimoyama Y, Hirohashi S: Dimeric E cadherin functions as a fundamental unit at the cell-cell adhesive interface in vivo. Nat Struct Biol 1999, in press. Chemical cross-linking studies directly on cells revealed that the formation of a calcium-dependent cis dimer is a necessity for the formation of frans dimers. This might also explain why several tumor cell lines, although expressing E-cadherin, exhibit little adhesion, as no dimeric form of E-cadherin could be detected on these cells.
29. Tamura K, Shan WS, Hendrickson WA, Colman DR, Shapiro L: Structure-function analysis of cell adhesion by neural (N-) cadherin. Neuron 1998, 20:1153-1163. This paper combines new X-ray structural data with mutagenesis data in order to the decipher the determinants of cadherin adhesion. The effects of structure- based mutations were checked in cell-aggregation assays, demonstrating the importance of a conserved hydrophobic cavity in which a likewise conserved tryptophan can dock. The authors took great care to ensure that the mutations did not affect the fold of the protein. The contradictory results concerning crystal contacts compared with previous works [17,18] were very frankly discussed.
30. 2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. EMBO J 1999, in press. The authors used two different and complementary techniques, electron microscopy and X-ray crystallography, to dissect the mechanism leading to cis and trans interactions in E-cadherin (see, also, [23]). Data are presented that demonstrate how calcium ions of different binding affinities participate in the association state of E-cadherin. The importance of a conserved tryptophan residue in frans interactions is shown and discrepancies with previous structural work on cadherins are discussed.
31. Ozawa M, Kemler R: Correct proteolytic cleavage is required for the cell adhesive function of uvomorufin. J Cell Biol 1990, 111:1645-1650.
32. Blaschuk OW, Sullivan R, David S, Pouliot Y: Identification of a cadherin cell adhesion recognition sequence. Dev Biol 1990, 139:227-229.
33. Tang L, Hung CP, Schuman EM: A role for the cadherin family of cell adhesion molecules in hippocampal long-term potentiation. Neuron 1998, 20:1165-1175. This paper implicates classic cadherins in synaptic plasticity. Hippocampal slices were employed to demonstrate that long-term potentiation can be reduced by blocking cadherin-mediated synaptic adhesion. Moreover, the adhesive state of cadherins in synapses seems to be sensitive to small physiological changes in extracellular calcium concentrations.
34. Leahy DJ: Implications of atomic-resolution structures for cell adhesion. Annu Rev Cell Dev Biol 1997, 13:363-393. An informative survey on recent X-ray structures from different cell adhesion proteins, including domains from cadherins, immunoglobulin superfamily members, integrins and fibronectin-like domains.
35. Carugo O, Argos P: Protein-protein crystal-packing contacts. Protein Sci 1997, 6:2261-2263.
36. Janin J: Specific versus non-specific contacts in protein crystals. Nat Struct Biol 1997, 4:973-974.
37. Spencer DM, Wandless TJ, Schreiber SL, Crabtree GR: Controlling signal transduction with synthetic ligands. Science 1993, 262:1019-1024.
38. Levenberg S, Katz BZ, Yamada KM, Geiger B: Long-range and selective autoregulation of cell-cell or cell-matrix adhesions by cadherin or integrin ligands. J Cell Sci 1998, 111:347-357.
39. Katz BZ, Levenberg S, Yamada KM, Geiger B: Modulation of cell-cell adherens junctions by surface clustering of the N-cadherin cytoplasmic tail. Exp Cell Res 1998, 243:415-424. The authors describe, in a way, a similar approach to [27••], as, in both cases, chimaeric cadherins, in which either the extracellular or the intracellular part is replaced, were used to force the clustering of the corresponding part. Here, N-cadherin ectodomains were replaced by nonactive subunits of the interleukin-2 receptor (IL-2R) and, therefore, adding beads covered with monoclonal antt-IL-2R antibodies could cluster cytosolic domains.
40. Chitaev NA, Troyanovsky SM: Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation. J Cell Biol 1998, 142:837-846. This paper depicts a calcium-independent E-cadherin cis dimer at the cell surface by co-immunoprecipitation experiments. Transforming cells with cadherins that were labeled with different epitopes identified frans dimers formed by interactions between cadherins from different cells.
41. Evans SV: SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules. J Mol Graphics 1993, 11:134-138.