Association of the AP-3 adaptor complex with clathrin

Science

Volumn 280, Issue 5362, 1998, Pages 431-434

  Dell'Angelica, Esteban C ^a   Klumperman, Judith ^b   Stoorvogel, Willem ^b   Bonifacino, Juan S ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADAPTOR PROTEIN AP 2; CLATHRIN; UNCLASSIFIED DRUG;

ARTICLE; HELA CELL; HUMAN; HUMAN CELL; IMMUNOELECTRON MICROSCOPY; IMMUNOFLUORESCENCE MICROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; AMINO ACID SEQUENCE; CLATHRIN; ENDOSOMES; FLUORESCENT ANTIBODY TECHNIQUE; HUMANS; INTRACELLULAR MEMBRANES; JURKAT CELLS; MICROSCOPY, CONFOCAL; MICROSCOPY, IMMUNOELECTRON; MOLECULAR SEQUENCE DATA; MONOMERIC CLATHRIN ASSEMBLY PROTEINS; NERVE TISSUE PROTEINS; PHOSPHOPROTEINS; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; VACUOLES;

MAMMALIA;

EID: 0032540419     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5362.431     Document Type: Article

References (33)

1. J. E. Rothman and F. T. Wieland, Science 272, 227 (1996); R. Schekman and L. Orci, ibid. 271, 1526 (1996).
2. J. E. Rothman and F. T. Wieland, Science 272, 227 (1996); R. Schekman and L. Orci, ibid. 271, 1526 (1996).
3. F. M. Brodsky, Trends Cell Biol. 7, 175 (1997); S. L. Schmid, Annu. Rev. Biochem. 66, 511 (1997).
4. F. M. Brodsky, Trends Cell Biol. 7, 175 (1997); S. L. Schmid, Annu. Rev. Biochem. 66, 511 (1997).
5. L. S. Newman, M. O. McKeever, H. J. Okano, R. B. Darnell, Cell 82, 773 (1995).
6. F. Simpson et al., J. Cell Biol. 133, 749 (1996); F. Simpson, A. A. Peden, L. Christopoulou, M. S. Robinson, ibid. 137, 835 (1997).
7. F. Simpson et al., J. Cell Biol. 133, 749 (1996); F. Simpson, A. A. Peden, L. Christopoulou, M. S. Robinson, ibid. 137, 835 (1997).
8. E. C. Dell'Angelica et al., EMBO J. 16, 917 (1997).
9. E. C. Dell'Angelica, C. E. Ooi, J. S. Bonifacino, J. Biol. Chem. 272, 15078 (1997).
10. H. R. Panek et al., EMBO J. 16, 4194 (1997).
11. C. E. Ooi et al., ibid., p. 4508; C. R. Cowles, G. Odorizzi, G. S. Payne, S. D. Emr, Cell 91, 109 (1997).
12. C. E. Ooi et al., ibid., p. 4508; C. R. Cowles, G. Odorizzi, G. S. Payne, S. D. Emr, Cell 91, 109 (1997).
13. J. D. Stepp, K. Huang, S. K. Lemmon, J. Cell Biol. 139, 1761 (1997); A. B. Seymour et al., Mol. Biol. Cell 8, 227a (abstr.) (1997).
14. J. D. Stepp, K. Huang, S. K. Lemmon, J. Cell Biol. 139, 1761 (1997); A. B. Seymour et al., Mol. Biol. Cell 8, 227a (abstr.) (1997).
15. S. Schröder and E. Ungewickell, J. Biol. Chem. 266, 7910 (1991); L. M. Traub, S. Kornfeld, E. Ungewickell, ibid. 270, 4933 (1995).
16. S. Schröder and E. Ungewickell, J. Biol. Chem. 266, 7910 (1991); L. M. Traub, S. Kornfeld, E. Ungewickell, ibid. 270, 4933 (1995).
17. W. Shih, A. Gallusser, T. Kirchhausen, ibid., p. 31083.
18. Peptide sequences matched segments of clathrin heavy chain encoded on human chromosome 17 (GenBank accession no. D21260) and all but the sequence IVLYAK (13) were distinct from those of a homolog encoded on human chromosome 22 (GenBank accession no. X95486).
19. Single-letter abbreviations for amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
20. E. C. Dell'Angelica, J. Klumperman, W. Stoorvogel, J. S. Bonifacino, unpublished observations.
21. J. G. Krupnick, O. B. Goodman Jr., J. H. Keen, J. L. Benovic, J. Biol. Chem. 272, 15011 (1997).
22. A. R. Ramjaun and P. S. McPherson, Mol. Biol. Cell 8, 93a (abstr.) (1997).
23. G. P. Vigers, R. A. Crowther, B. M. Pearse, EMBO J. 5, 2079 (1986); O. B. Goodman Jr., J. G. Krupnick, V. V. Gurevich, J. L. Benovic, J. H. Keen, J. Biol. Chem. 272, 15017 (1997).
24. G. P. Vigers, R. A. Crowther, B. M. Pearse, EMBO J. 5, 2079 (1986); O. B. Goodman Jr., J. G. Krupnick, V. V. Gurevich, J. L. Benovic, J. H. Keen, J. Biol. Chem. 272, 15017 (1997).
25. 2 for 12 to 14 hours at 4°C.
26. W. Stoorvogel, V. Oorschot, H. J. Geuze, J. Cell Biol. 132, 21 (1996).
27. C to introduce a stop codon at position 886 of β3A.
28. C coupled to Affi-Gel 15 (Bio-Rad). Bound proteins were washed with 0.1% (w/v) saponin in phosphate-buffered saline and then eluted with 0.1 M glycine (pH 2.5).
29. I. S. Näthke et al., Cell 68, 899 (1992).
30. C coupled to Affi-Gel 15 beads. Bound proteins were eluted by heating the beads at 95°C for 5 min in the presence of 1% (w/v) SDS, 10 mM dithiothreitol, 0.1 M tris-HCl (pH 7.4). Samples were diluted 1:20 with 50 mM tris-HCl buffer (pH 7.4) containing 1% (w/v) Triton X-100, 0.3 M NaCl, 10 mM iodoacetamide, 5 mM EDTA, 0.1% (w/v) BSA and immunoprecipitated (5) with the X22 antibody [F. M. Brodsky, J. Cell Biol. 101, 2047 (1985)].
31. 2, 10% (v/v) glycerol, 0.1% (w/v) BSA, and 0.05% (w/v) Triton X-100 and centrifuged at 120,000g for 30 min at 4°C to remove protein aggregates.
32. J. W. Slot, H. J. Geuze, Gigengack, S., G. E. Lienhard, D. E. James, J. Cell Biol. 113, 123 (1991).
33. We thank M.-C. Foumier and V. Oorschot for excellent technical assistance; L. Green and E. Eisenberg for advice on the purification of clathrin; F. Brodsky, L. Samelson, E. Ungewickell, and W. Zhang for generous gifts of reagents; and J. Donaldson, J. Lippincott-Schwartz, C. E. Ooi, and G. Storz for critical review of the manuscript.