Recognition of accessory protein motifs by the γ-adaptin ear domain of GGA3

Nature Structural Biology

Volumn 10, Issue 8, 2003, Pages 599-606

  Miller, Gregory J ^a   Mattera, Rafael ^b   Bonifacino, Juan S ^b   Hurley, James H ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ALANINE; ARGININE; LEUCINE; MEMBRANE PROTEIN; PHENYLALANINE; PROLINE; PROTEIN; RABAPTIN 5; UNCLASSIFIED DRUG; VALINE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HYDROPHOBICITY; MEMBRANE TRANSPORT; MEMBRANE VESICLE; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE;

ADAPTOR PROTEIN COMPLEX 1; ADAPTOR PROTEIN COMPLEX GAMMA SUBUNITS; ADAPTOR PROTEINS, VESICULAR TRANSPORT; ADP-RIBOSYLATION FACTORS; AMINO ACID SEQUENCE; BINDING SITES; CARRIER PROTEINS; CLATHRIN-COATED VESICLES; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HUMANS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TRANS-GOLGI NETWORK;

EID: 0042991385     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb953     Document Type: Article

References (32)

1. Kirchhausen, T. Adaptors for clathrin-mediated traffic. Annu. Rev. Cell Dev. Biol. 15, 705-732 (1999).
2. Robinson, M.S. & Bonifacino, J.S. Adaptor-related proteins. Curr. Opin. Cell Biol. 13, 444-453 (2001).
3. Boman, A.L., Zhang, C.J., Zhu, X. & Kahn, R.A. A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol. Biol. Cell 11, 1241-1255 (2000).
4. Dell'Angelica, E.C. et al. GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J. Cell Biol. 149, 81-94 (2000).
5. Hirst, J. et al. A family of proteins with γ-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J. Cell Biol. 149, 67-80 (2000).
6. Poussu, A., Lohi, O. & Lehto, V.P. Vear, a novel Golgi-associated protein with VHS and γ-adaptin 'ear' domains. J. Biol. Chem. 275, 7176-7183 (2000).
7. Nielsen, M.S. et al. The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. EMBO J. 20, 2180-2190 (2001).
8. Puertollano, R., Aguilar, R.C., Gorshkova, I., Crouch, R.J. & Bonifacino, J.S. Sorting of mannose 6-phosphate receptors mediated by the GGAs. Science 292, 1712-1716 (2001).
9. Zhu, Y., Doray, B., Poussu, A., Lehto, V.P. & Kornfeld, S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science 292, 1716-1718 (2001).
10. Takatsu, H., Katoh, Y., Shiba, Y. & Nakayama, K. Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276, 28541-28545 (2001).
11. Slepnev, V.I. & De Camilli, P. Accessory proteins in clathrin-dependent synaptic vesicle endocytosis. Nat. Rev. Neurosci. 1, 161-172 (2000).
12. Benmerah, A., Begue, B., Dautry-Varsat, A. & Cerf-Bensussan, N. The ear of α-adaptin interacts with the COOH-terminal domain of the Eps 15 protein. J. Biol. Chem. 271, 12111-12116 (1996).
13. Brett, T.J., Traub, L.M. & Fremont, D.H. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure 10, 797-809 (2002).
14. Owen, D.J. et al. A structural explanation for the binding of multiple ligands by the α-adaptin appendage domain. Cell 97, 805-815 (1999).
15. Owen, D.J., Vallis, Y., Pearse, B.M., McMahon, H.T. & Evans, P.R. The structure and function of the β2-adaptin appendage domain. EMBOJ. 19, 4216-4227 (2000).
16. Mattera, R., Arighi, C.N., Lodge, R., Zerial, M. & Bonifacino, J.S. Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. EMBO J. 22, 78-88 (2003).
17. Mills, I.G. et al. EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. J. Cell Biol. 160, 213-222 (2003).
18. Liu, W.W.Y. et al. Binding partners for the COOH-terminal appendage domains of the GGAs and γ-adaptin. Mol. Biol. Cell 14, 2385-2398 (2003).
19. Duncan, M.C., Costaguta, G. & Payne, G.S. Yeast epsin-related proteins required for Golgi-endosome traffic define a γ-adaptin ear-binding motif. Nat. Cell Biol. 5, 77-81 (2003).
20. Kent, H.M., McMahon, H.T., Evans, P.R., Senmerah, A. & Owen, D. J. γ-adaptin appendage domain: structure and binding site for Eps15 and γ-synergin. Structure 10, 1139-1148 (2002).
21. Nogi, T. et al. Structural basis for the accessory protein recruitment by the γ-adaptin ear domain. Nat. Struct. Biol. 9, 527-531 (2002).
22. Page, L.J., Sowerby, P.J., Lui, W.W. & Robinson, M.S. γ-synergin: an EH domain-containing protein that interacts with γ-adaptin. J. Cell Biol. 146, 993-1004 (1999).
23. Collins, B.M., Praefcke, G.J.K., Robinson, M.S. & Owen, D.J. Structural basis for binding of accessory proteins by the appendage domain of GGAs. Nat. Struct. Biol. advance online publication, 13 July 2003 (doi:10.1038/nsb955).
24. Sheffield, P., Garrard, S. & Derewenda, Z. Overcoming expression and purification problems of RhoGDI using a family of 'parallel' expression vectors. Protein Expr. Purif. 15, 34-39 (1999).
25. Dell'Angelica, E.C., Klumperman, J., Stoorvogel, W. & Bonifacino, J.S. Association of the AP-3 adaptor complex with clathrin. Science 280, 431-434 (1998).
26. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
27. Terwilliger, T.C. & Berendzen, J. Correlated phasing of multiple isomorphous replacement data. Acta Crystallogr. D 52, 749-757 (1996).
28. Terwilliger, T.C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
29. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
30. Brunger, A.T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
31. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
32. Merritt, E.A. & Bacon, D.J. Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).