Bimodal interaction of coatomer with the p24 family of putative cargo receptors

Science

Volumn 273, Issue 5280, 1996, Pages 1396-1399

  Fiedler, Klaus ^a   Veit, Michael ^a   Stamnes, Mark A ^a   Rothman, James E ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN P24; MEMBRANE RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN;

EID: 0029796074     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5280.1396     Document Type: Article

References (37)

1. JE. Rothman and F, T. Wieland, Science 272 227 (1996).
2. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
3. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
4. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
5. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
6. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
7. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
8. R. Duden et al., J. Biol. Chem. 269, 24486 (1994); Q Guo. E. Vasile, M. Krieger, J. Cell Biol. 125 1213 (199 4) ; M. Hosobuchi, T. Kreis, R. Schekman, Nature 360, 603 (1992); J. Ostermann et al., Cell 75, 1015 (1993); R. Pepperkok et al., ibid. 74, 71 (1993); F. Peter, H. Plutner, H. Zhy, T. E. Kreis, W. E. Balch, J. Cell Biol. 122, 1155 (1993); G, Stenbeck et al., FEBS Lett. 314 195 (1992).
9. S. Y. Bednarek et al., Cell 83, 1183 (1995).
10. M. G. Waters, T. Serafini, J. E. Rothman, Nalure 349, 248 (1991).
11. P. Cosson and F. Letoumeur, Science 263, 1629 (1994).
12. F. Letourneur et al., Cell 79, 1199 (1994).
13. P. Cosson, C. Demolliere, S. Hennecke, R. Duden, F. Letourneur, EMBO J, 15, 1792 (1996).
14. I. Wada et al., J. Biol. Chem. 266, 19599 (1991).
15. M. A. Stamnes et al., Proc. Natl. Acad Sci. U.S.A. 92, 8011 (1995).
16. F. Schimmoller et al., EMBO J. 14, 1329 (1995).
17. C. Barlowe et al., Cell 77, 895 (1994).
18. Abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I1 lle; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr; and X, any amino acid.
19. T. M. Nilsson, M. R. Jackson, P. A. Peterson, Cell 58, 707 (1989).
20. M. R. Jackson, T. Nilsson, P. A. Peterson, EMBO J. 9, 3153 (1990).
21. S. te Heesen, B. Janetzky, L. Lehle, M. Aebi, ibid. 11, 2071 (1992).
22. S. Paabo, B. M. Bhat. W. S. M. Wold, P. A. Peterson, Cell 50, 311 (1987).
23. M. Lowe and T. E. Kreis, J. Biol. Chem. 270, 31364 (1995).
24. K. Fiedler and K. Simons. Cell 81, 309 (1995).
25. S. Ponnambalam, C. Rabouille, J. P. Luzio. T. Nilsson, G. Warren, J. Cell Biol. 125, 253 (1994).
26. M. C. Pascale et al., J. Biol. Chem. 267, 25196 (1992).
27. D. J. Leahy, R. Axel, W. A. Hendrickson, Cell 68, 1145 (1992).
28. R. W. Doms et al., J. Cell Biol. 107, 89 (1988).
29. S. M. Hurtley and A. Helenius.Annu. Rev. Cell biol. 5, 277 (1989).
30. 2. The beads were further washed with 1 ml of buffer A containing 1,3 M NaCl followed by 1 ml of buffer A.
31. CHO extracts were prepared from ~3 ml of centri-fuged cells with 40 ml of buffer A containing leupeptin and antipain each at 20 μg/ml. The extracts were rotated for 30 min at 4°C. Insoluble material was removed by centrifugation for 45 min at 180,000g and 4°C, and the resulting supernatants were frozen in liquid nitrogen. Thawed CHO extract was recentrifuged and 800 μl) in buffer A were incubated for 3 hours at 4°C (with rotation) with the beads containing bound GST fusion proteins. The beads were washed three times with 1 ml of buffer A and once with 50mM Hepes (pH 7.2). After aspiration with a Hamilton syringe, bound proteins were eluted by boiling in reducing SDS sample buffer. SDS-polyacrylamide gel electrophoresis and immunoblot analysis by enhanced chemiluminescence (ECL, Amarsham) were performed as described [S. Hara-Kuge et al., J. Cell Biol. 124, 883 (1994)]. Antibodies were used at the following dilutions: anti-α-COP (883, affinity-purified), 1:1500; anti-β-COP (M3A5, ascites), 1:800; anti-β'-COP (C1PL, affinity-purified), 1:3000; anti-γ-COP (serum), 0.4 μg/ml; anti-ε-COP (affinity-purified), 50 ng/ml; and anti-ζ-COP (affinity-purified), 20 ng/ml.
32. J. Devereux, P. Haebeli, O. Smithies, Nucleic Acid Res. 12, 387 (1984).
33. GenBank-EMBL accession numbers: hp24a (T27390, F06012, T34121, R14234, T27339, T11000, T48545); hp24b (T48838, R25915, T17481); hp24c (T32238); hp24d (T98284); hp24e (F07445); chop24a (U26264); gp25l (X53592); ap24a (Z34726); ap24b (T46519); Emp24p (X67317); yp24b (L22015); yp24c (U00059); yp24d (L22015); yp24e (X87331, T36996); yp24f (Z48432); and yp24g (Z49810).
34. The constructs encoding wild-type GST-WBP1 (GST-KKLETFKKTN) (72), mutant GST-WBP1 (GST-KKLETFSSTN). wild-type E19 (GST-KYKSRRSFIDEKKMP), and mutant E19 (GST-KYKSRRSHDESSMP) in the pGEX-3X vector were described previously (5). All procedures were performed as described (24, 25).
35. The CD8 chimeras were constructed by the poly-merase chain reaction such that the 165 amino acids of the human CD8 extracellular domain were preserved. Codon 166 was changed to glycine to introduce a unique Apa I restriction site and was followed by a conserved proline, a stop codon, and an Eco Rl site. Oligonucleotides encoding the COOH-terminal 34 amino acids of chop24a [RWLWSFFEALVL-VAMTLGQIYYLKR(F/A)(F/A)EVRRVV] (12), preceded by an Apa I site and followed by a stop codon and an Eco Rl site, were subcloned into the CDB construct and inserted into the pECE vector [L. Ellis et al, Cell 45, 721 (1986)]. Sequences were verified by DNA sequencing. Transfection of COS- 7 cells was performed with Lipofectin and Lipofectamine (Gibco BRL) for immunofluorescence and pulse-chase analysis, respectively. The OKT8 monoclonal antibody to CD8 (Ortho) and fluorescein-conjugated goat antibodies to mouse immunoglobulin (Molecular Probes) were used at a dilution of 1/30 and 1/100, respectively, for immunofluorescence.
36. Pulse-chase analysis and immunoprecipitation with the OKT8 monoclonal antibody were performed essentially as described [M. R. Jackson, T. Nilsson, P. A. Peterson, J. Cell Biol. 121, 317 (1993)] but with protein G-agarose (Boehringer).
37. We thank T. Söllner, C. Blobel, and M. Craighead for discussions; C. Harter, F. Wieland, and T. Kreis for antibodies; F. Letourneur and P. Cosson for the GST-WBP1 and GST-E19 constructs; S. Ponnambalam and T. Nilsson for the CD8 cDNA construct: and M. Spiess for the pECE vector. Supported by NIH and the Mathers Charitable Foundation (J.E.R.); the Human Frontier Science Program Organization and the Swiss National Science Foundation (K.F.); and the Deutsche Forschungsgemeinschaft (M.V.).