Comparison of CD45 Extracellular Domain Sequences from Divergent Vertebrate Species Suggests the Conservation of Three Fibronectin Type III Domains

Journal of Immunology

Volumn 157, Issue 4, 1996, Pages 1569-1575

  Okumura, Meinoshin ^a   Matthews, R James ^a,d   Robb, Bruce ^a   Litman, Gary W ^b   Bork, Peer ^c   Thomas, Matthew L ^a,e  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF SOUTH FLORIDA   (United States)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d CARDIFF UNIVERSITY   (United Kingdom)

^e HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; FIBRONECTIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; CHICKEN; COMPARATIVE STUDY; GENETICS; GLYCOSYLATION; HUMAN; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE; RNA SPLICING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SHARK; SPECIES DIFFERENCE; VERTEBRATE;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD45; CHICKENS; EVOLUTION, MOLECULAR; FIBRONECTINS; GLYCOSYLATION; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RNA SPLICING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SHARKS; SPECIES SPECIFICITY; VERTEBRATES;

EID: 0030586604     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (52)

1. Mourey, R. J., and J. E. Dixon. 1994. Protein tyrosine phosphatases: characterization of extracellular and intracellular domains. Curr. Opin. Genet. Dev. 4:31.
2. Stone, R., and J. Dixon. 1994. Protein-tyrosine phosphatases. J. Biol. Chem. 269:31323.
3. Gebbink, M. F. B. G., G. C. M. Zondag, R. W. Wubbolts, R. L. Beijersbergen, I. van Etten, and W. H. Moolenaar. 1993. Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase. J. Biol. Chem. 268:16101.
4. Brady-Kalnay, S. M., A. J. Flint, N. K. Tonks, A. Singer, and H. Westphal. 1993. Homophilic binding of PTPμ, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. J. Cell Biol. 122:961.
5. Sap, J., Y. Jiang, D. Friedlander, M. Grumet, and J. Schlessinger. 1994. Receptor tyrosine phosphatase R-PTP-κ mediates homophilic binding. Mol. Cell. Biol. 14:1.
6. Milev, P., D. Friedlander, T. Sakurai, L. Karthikeyan, M. Flad, R. Margolis, and M. Grumet. 1994. Interactions of the chondroitin sulfate proteoglycan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules. J. Cell Biol. 127:1703.
7. Peles, E., M. Nativ, P. L. Campbell, T. Sakurai, R. Martinez, S. Lev, D. O. Clary, J. Schilling, G. Barnea, G. D. Plowman, M. Grumet, and J. Schlessinger. 1995. The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin. Cell 82:251.
8. Pingel, J. T., and M. L. Thomas. 1989. Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell 58:1055.
9. Justement, L. B., K. S. Campbell, N. C. Chien, and J. C. Cambier. 1991. Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45. Science 252:1839.
10. Peyron, J. F., S. Verma, R. de Waal Malefyt, J. Sancho, C. Terhorst, and H. Spits. 1991. The CD45 protein tyrosine phosphatase is required for the completion of the activation program leading to lymphokine production in the Jurkat human T cell line. Int. Immunol. 3:1357.
11. + T-cell clones deficient in the expression of the CD45 protein tyrosine phosphatase have impaired responses to T-cell receptor stimuli. Mol. Cell. Biol. 11:4415.
12. Koretzky, G. A., J. Picus, M. L. Thomas, and A. Weiss. 1990. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature 346:66.
13. Kishihara, K., J. Penninger, V. A. Wallace, T. M. Kundig, K. Kawai, A. Wakeham, E. Timms, K. Pfeffer, P. S. Ohashi, M. L. Thomas, C. Furlonger, C. J. Paige, and T. W. Mak. 1993. Normal B lymphocyte development but impaired T cell maturation in CD45-exon6 protein tyrosine phosphatase-deficient mice. Cell 74:143.
14. Cahir McFarland, E. D., T. R. Hurley, J. T. Pingel, B. M. Sefton, A. Shaw, and M. L. Thomas. 1993. Correlation between Src-family member regulation by the protein tyrosine phosphatase, CD45, and transmembrane signaling through the T-cell receptor. Proc. Natl. Acad. Sci. USA 90:1402.
15. Sieh, M., J. B. Bolen, and A. Weiss. 1993. CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck. EMBO J. 12:315.
16. fyn couples the T cell antigen receptor to pathways of diacylglycerol production, protein kinase C activation and calcium influx. EMBO J. 11:4887.
17. lck by the leukocyte common antigen (CD45). Oncogene 5:809.
18. fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphalase. Eur. J. Immunol. 22:1173.
19. Pingel, J. T., E. D. Cahir McFarland, and M. L. Thomas. 1994. Activation of CD45-deficient T cell clones by lectin mitogens but not anti-Thy-1. Int. Immunol. 6:169.
20. Brown, W. R. A., A. N. Barclay, C. A. Sunderland, and A. F. Williams. 1981. Identification of a glycophorin-like molecules at the cell surface of rat thymocytes. Nature 289:456.
21. Hall, L. R., M. Streuli, S. F. Schlossman, and H. Saito. 1988. Complete exonintron organization of the human leukocyte common antigen (CD45) gene. J. Immunol. 141:2781.
22. Saga, Y., J.-S. Tung, F.-W. Shen, T. C. Pancoast, and E. A. Boyse. 1988. Organization of the Ly-5 gene. Mol. Cell. Biol. 8:4889.
23. Johnson, N. A., C. M. Meyer, J. T. Pingel, and M. L. Thomas. 1989. Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene. J. Biol. Chem. 264:6220.
24. 2-terminus. EMBO J. 6:1259.
25. Thomas, M. L., P. J. Reynolds, A. Chain, Y. Ben-Neriah, and I. S. Trowbridge. 1987. B-cell variant of mouse T200 (Ly-5): evidence for alternative mRNA splicing. Proc. Natl. Acatl. Sci. USA 84:5360.
26. Saga, Y., J.-S. Tung, F.-W. Shen, and E. A. Boyse. 1987. Alternative use of 5′ exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages. Proc. Natl. Acad. Sci. USA 84:5364.
27. Streuli, M., L. R. Hall, Y. Saga, S. F. Schlossman, and H. Saito. 1987. Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens. J. Exp. Med. 166:1548.
28. Thomas, M. L. 1989. The leukocyte common antigen family. Annu. Rev. Immunol. 7:339.
29. Powell, L. D., D. Sgroi, E. R. Sjoberg, I. Stamenkovic, and A. Varki. 1993. Natural ligands of the B cell adhesion molecule CD22β carry N-linked oligosaccharides with α-2,6-sialic acids that are required for recognition. J. Biol. Chem. 268:7019.
30. Munro, S., B. J. E. G. Bast, K. J. Colley, and T. F. Tedder. 1992. The B lymphocyte surface antigen CD75 is not an α-2,6-sialytransferase but is a carbohydrate antigen, the production of which requires the enzyme. Cell 68:1003.
31. Stamenkovic, I., D. Sgroi, A. Aruffo, M. S. Sy, and T. Anderson. 1991. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α-2,6-sialytransferase, CD75, on B cells. Cell 66:1133.
32. Lefrancois, L. 1987. Expression of carbohydrate differentiation antigens during ontogeny of the murine thymus. J. Immunol. 139:2220.
33. Chui, D., C. J. Ong, P. Johnson, H-S. Teh, and J. D. Marth. 1994. Specific CD45 isoforms differentially regulate T cell receptor signaling. EMBO J. 13:798.
34. Novak, T. J., D. Farber, D. Leitenberg, S-C. Hong, P. Johnson, and K. Bottomly. 1994. Isoforms of the transmembrane tyrosine phosphatase CD45 differentially affect T cell recognition. Immunity 1:109.
35. Ong, C. J., D. Chui, H-S. Teh, and J. D. Marth. 1994. Thymic CD45 tyrosine phosphatase regulates apoptosis and MHC-restricted negative selection. J. Immunol. 152:3793.
36. McKenney, D. W., H. Onodera, L. Gorman, T. Mimura, and D. M. Rothstein. 1995. Distinct isoforms of the CD45 protein-tyrosine phosphatase differentially regulate interleukin 2 secretion and activation signal pathways involving Vav in T cells. J. Biol. Chem. 270:24949.
37. Bork, P., and R. F. Doolittle. 1993. Fibronectin type III modules in the receptor phosphatase CD45 and tapeworm antigens. Protein Sci. 2:1185.
38. Kokubu, F., K. Hinds, R. Litman, M. J. Shamblott, and G. W. Litman. 1988. Complete structure and organization of immunoglobulin heavy chain constant region genes in a phylogenetically primitive vertebrate. EMBO J. 7:1979.
39. Matthews, R. J., E. D. Cahir, and M. L. Thomas. 1990. Identification of an additional member of the protein-tyrosine-phosphatase family: evidence for alternative slicing in the tyrosine phosphatase domain. Proc. Natl. Acatl. Sci. USA 87:4444.
40. Matthews, R. J., D. B. Bowne, E. Flores, and M. L. Thomas. 1992. Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol. Cell. Biol. 12:2396.
41. Koonin, E. V., P. Bork, and C. Sander. 1994. Yeast chromosome III: new gene functions. EMBO J. 13:493.
42. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673.
43. Kozak, M. 1991. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol. 115:887.
44. Fang, K. S., K. Barker, M. Sudol, and H. Hanafusa. 1994. A transmembrane protein-tyrosine phosphatase contains spectrin-like repeats in its extracellular domain. J Biol. Chem. 269:14056.
45. Jackson, D. I., and A. N. Barclay. 1989. The extra segments of sequence in rat leucocyte common antigen (L-CA) are derived by alternative splicing of only three exons and show extensive O-linked glycosylation. Immunogenetics 29:281.
46. Leahy, D. J., W. Hendrickson, I. Aukhil, and H. Erickson. 1992. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258:987.
47. Main. A., T. Harvey, M. Baron, J. Boyd, and I. Campbell. 1992. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71:671.
48. Bork, P., L. Holm, and C. Sander. 1994. The immunoglobulin fold: structural classification, sequence patterns and common core. J. Mol. Biol. 242:309.
49. Huber, A., Y. Wang, A. J. Bieber, and P. J. Bjorkman. 1994. The crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A. Neuron 12:717.
50. Cahir McFarland, E. D., and M. L. Thomas. 1995. CD45 protein tyrosine phosphatase associates with the WW domain-containing protein, CD45AP, through the transmembrane region. J. Biol. Chem. 270:28103.
51. Shamblott, M. J., and G. W. Litman. 1989. Genomic organization and sequences of immunoglobulin light chain genes in a primitive vertebrate suggest coevolution of immunoglobulin gene organization. EMBO J. 8:3733.
52. Rast, J., and G. Litman. 1995. T-cell receptor gene homologs are present in the most primitive jawed vertebrates. Proc. Natl. Acad. Sci. USA 91:9248.