Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat

Nature

Volumn 419, Issue 6904, 2002, Pages 271-277

  Bi, Xiping ^a   Corpina, Richard A ^a   Goldberg, Jonathan ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; MOLECULES; POLYMERIZATION;

VESICLES;

NATURAL SCIENCES;

GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; PHOSPHOLIPID; RECOMBINANT PROTEIN; SNARE PROTEIN;

BIOCHEMISTRY; VESICLE;

ARTICLE; BINDING SITE; CRYSTALLIZATION; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; HYDROLYSIS; MEMBRANE VESICLE; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN SYNTHESIS; SACCHAROMYCES CEREVISIAE; YEAST;

AMINO ACID SEQUENCE; BINDING SITES; BIOLOGICAL TRANSPORT; COP-COATED VESICLES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MONOMERIC GTP-BINDING PROTEINS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0037136560     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01040     Document Type: Article

References (50)

1. Mellman, I. & Warren, G. The road taken: past and future foundations of membrane traffic. Cell 100, 99-112 (2000).
2. Kirchhausen, T. Three ways to make a vesicle. Nature Rev. Mol. Cell Biol. 1, 187-198 (2000).
3. Serafini, T. et al. ADP-ribosylation factor is a subunit of the coat of (Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67, 239-253 (1991).
4. Donaldson, J. G., Cassel, D., Kahn, R. A. & Klausner, R. D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein β-COP to Golgi membranes. Proc. Natl Acad. Sci. USA 89, 6408-6412 (1992).
5. Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907 (1994).
6. Tanigawa, G. et al. Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123, 1365-1371 (1993).
7. Yoshihisa, T., Barlowe, C. & Schekman, R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259, 1466-1468 (1993).
8. Antonny, B., Madden, D., Hamamoto, S., Orci, L. & Schekman, R. Dynamics of the COPII coat with GTP and stable analogues. Nature Cell Biol. 3, 531-537 (2001).
9. Nagahama, M. et al. Av-SNARE implicated in intra-Golgi transport. J. Cell Biol. 133, 507-516 (1996).
10. Springer, S. & Schekman, R. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 281, 698-700 (1998).
11. Grabowski, R. & Gallwitz, D. High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5P, to wild-type and mutant Sly1p, a modulator of transport vesicle docking. FEBS Lett. 411, 169-172 (1997).
12. Matsuoka, K. et al. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93, 263-275 (1998).
13. Nakano, A., Brada, D. & Schekman, R. A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast. J. Cell Biol. 107, 851-863 (1988).
14. Barlowe, C. & Schekman, R. SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365, 347-349 (1993).
15. Weissman, J. T., Plutner, H. & Balch, W. E. The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic 2, 465-475 (2001).
16. Huang, M. et al. Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH2 terminus in ER export. J. Cell Biol, 155, 937-948 (2001).
17. Amor, J. C., Harrison, D. H., Kahn, R. A. & Ringe, D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704-708 (1994).
18. Antonny, B., Beraud-Dufour, S., Chardin, P. & Chabre, M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36, 4675-4684 (1997).
19. Goldberg, J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248 (1998).
20. Beraud-Dufour, S., Paris, S., Chabre, M. & Antonny, B. Dual interaction of ADP ribosylation factor 1 with Sec7 domain and with lipid membranes during catalysis of guanine nucleotide exchange. J. Biol Chem. 274, 37629-37636 (1999).
21. Lederkremer, G. Z. et al. Structure of the Sec23p/24p and Sec13p/31p complexes of COPII. Proc. Natl Acad. Sci. USA 98, 10704-10709 (2001).
22. Matsuoka, K., Schekman, R., Orci, L. & Heuser, J. E. Surface structure of the COPII-coated vesicle. Proc. Natl Acad. Sci. USA 98, 13705-13709 (2001).
23. Kuehn, M. J., Herrmann, J. M. & Schekman, R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391, 187-190 (1998).
24. Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C. & Balch, W. E. Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol. 141, 61-70 (1998).
25. Peng, R., Grabowski, R., De Antoni, A. & Gallwitz, D. Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proc. Natl Acad. Sci. USA 96, 3751-3756 (1999).
26. Votsmeier, C. & Gallwitz, D. An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export. EMBO J. 20, 6742-6750 (2001).
27. Martinez-Menarguez, J. A., Geuze, H. J., Slot, J. W. & Klumperman, J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98, 81-90 (1999).
28. Balch, W. E., McCaffery, J. M., Plutner, H. & Farquhar, M. G. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 76, 841-852 (1994).
29. ter Haar, E., Musacchio, A., Harrison, S. C. & Kirchhausen, T. Atomic structure of clathrin: a β propeller terminal domain joins an α zigzag linker. Cell 95, 563-573 (1998).
30. Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R. & Owen, D. J. Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523-535 (2002).
31. Huang, M., Weissman, J. T., Wang, C., Balch, W. E. & Wilson, I. A. Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding. Acta Crystallogr. D 58, 700-703 (2002).
32. Paris, S. et al. Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J. Biol. Chem. 272, 22221-22226 (1997).
33. Goldberg, J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893-902 (1999).
34. Pasqualato, S., Menetrey, J., Franco, M. & Cherfils, J. The structural GDP/GTP cycle of human Arf6. EMBO Rep. 2, 234-238 (2001).
35. Hanzal-Bayer, M., Renault, L., Roversi, P., Wittinghofer, A. & Hillig, R. C. The complex of Arl2-GTP and PDEδ: from structure to function. EMBO J. 21, 2095-2106 (2002).
36. Shimoni, Y. et al. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J. Cell Biol. 151, 973-984 (2000).
37. Thompson, J. D., Higgins, D. G. & Gibson, T. J. 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, 4673-4680 (1994).
38. Ponting, C. P., Aravind, L., Schultz, J., Bork, P. & Koonin, E. V. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289, 729-745 (1999).
39. Robinson, R. C. et al. Domain movement in gelsolin: a calcium-activated switch. Science 286, 1939-1942 (1999).
40. Peng, R., De Antoni, A. & Gallwitz, D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J. Biol. Chem. 275, 11521-11528 (2000).
41. Franco, M., Chardin, P., Chabre, M. & Paris, S. Myristoylation is not required for GTP-dependent binding of ADP-ribosylation factor ARF1 to phospholipids. J. Biol. Chem. 268, 24531-24534 (1993).
42. Franco, M., Chardin, P., Chabre, M. & Paris, S. Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor. J. Biol. Chem. 271, 1573-1578 (1996).
43. Randazzo, P. A. Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4, 5-bisphosphate. J. Biol. Chem. 272, 7688-7692 (1997).
44. Scheffzek, K., Ahmadian, M. R. & Wittinghofer, A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257-262 (1998).
45. Shaywitz, D. A., Espenshade, P. J., Gimeno, R. E. & Kaiser, C. A. COPII subunit interactions in the assembly of the vesicle coat. J. Biol. Chem. 272, 25413-25416 (1997).
46. Otwinoski, W. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
47. Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
48. Collaborative Computational Project Number 4 The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
49. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
50. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).