Molecular model for a complete clathrin lattice from electron cryomicroscopy

Nature

Volumn 432, Issue 7017, 2004, Pages 573-579

  Fotin, Alexander ^a   Cheng, Yifan ^a   Sliz, Piotr ^a   Grigorieff, Nikolaus ^c   Harrison, Stephen C ^b   Kirchhausen, Tomas ^a   Walz, Thomas ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c BRANDEIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; LATTICE VIBRATIONS; MATHEMATICAL MODELS; MOLECULAR BIOLOGY;

CLATHRIN LATTICE; HOMOLOGY; VESICLES;

CELL MEMBRANES;

CLATHRIN;

PROTEIN;

ARTICLE; CELL MEMBRANE TRANSPORT; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; IMAGE RECONSTRUCTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; CATTLE; CLATHRIN; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY;

TRISKELION;

EID: 10344262047     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03079     Document Type: Article

References (41)

1. Kirchhausen, T. Clathrin. Annu. Rev. Biochem. 69, 699-727 (2000).
2. Robinson, M. S. Adaptable adaptors for coated vesicles. Trends Cell Biol. 14, 167-174 (2004).
3. Brodsky, F. M., Chen, C. Y., Knuehl, C., Towler, M. C. & Wakeham, D. E. Biological basket weaving: formation and function of clathrin-coated vesicles. Annu. Rev. Cell Dev. Biol. 17, 517-568 (2001).
4. Crowther, R. A., Finch, J. T. & Pearse, B. M. On the structure of coated vesicles. J. Mol. Biol. 103, 785-798 (1976).
5. Kirchhausen, T. & Harrison, S. C. Protein organization in clathrin trimers. Cell 23, 755-761 (1981).
6. Ungewickell, E. & Branton, D. Assembly units of clathrin coats. Nature 289, 420-422 (1981).
7. Kirchhausen, T., Harrison, S. C. & Heuser, J. Configuration of clathrin trimers: Evidence from electron microscopy. J. Ultrastruct. Mol. Struct. Res. 94, 199-208 (1986).
8. Ungewickell, E. Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. EMBO J. 8, 1401-1408 (1983).
9. Kirchhausen, T., Harrison, S. C., Parham, P. & Brodsky, F. M. Location and distribution of the light chains in clathrin trimers. Proc. Natl Acad. Sci. USA 80, 2481-2485 (1983).
10. Kirchhausen, T. et al. Clathrin light chains LCA and LCB are similar, polymorphic and share repeated heptad motifs. Science 236, 320-324 (1987).
11. Jackson, A. P., Seow, H. F., Holmes, N., Drickamer, K. & Parham, P. Clathrin light chains contain brain-specific insertion sequences and a region of homology with intermediate filaments. Nature 326, 154-159 (1987).
12. Vigers, G. P., Crowther, R. A. & Pearse, B. M. Three-dimensional structure of clathrin cages in ice. EMBO J. 5, 529-534 (1986).
13. Vigers, G. P., Crowther, R. A. & Pearse, B. M. Location of the 100 kd-50 kd accessory proteins in clathrin coats. EMBO J. 5, 2079-2085 (1986).
14. Smith, C. J., Grigorieff, N. & Pearse, B. M. Clathrin coats at 21 Å resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17, 4943-4953 (1998).
15. Musacchio, A. et al. Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography. Mol. Cell 3, 761-770 (1999).
16. 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).
17. Ybe, J. A. et al. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature 399, 371-375 (1999).
18. Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
19. Liu, S.-H., Wong, M. L., Craik, C. S. & Brodsky, F. M. Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs. Cell 83, 257-267 (1995).
20. Kirchhausen, T. & Toyoda, T. Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers. J. Biol. Chem. 268, 10268-10273 (1993).
21. Scarmato, P. & Kirchhausen, T. Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. J. Biol. Chem. 265, 3661-3668 (1990).
22. Nathke, I. S. et al. Folding and trimerization of clathrin subunits at the triskelion hub. Cell 68, 899-910 (1992).
23. Chen, C. Y. et al. Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. EMBO J. 21, 6072-6082 (2002).
24. Ungewickell, E. et al. Role of auxilin in uncoating clathrin-coated vesicles. Nature 378, 632-635 (1995).
25. Heuser, J. Three-dimensional visualization of coated vesicle formation in fibroblasts. J. Cell Biol. 84, 560-583 (1980).
26. Ehrlich, M. et al. Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell 118, 591-605 (2004).
27. Fotin, A. et al. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature doi:10.1038/nature03078 (this issue).
28. Matsui, W. & Kirchhausen, T. Stabilization of clathrin coats by the core of the clathrin-associated protein complex AP-2. Biochemistry 29, 10791-10798 (1990).
29. Thon, F. Zur Defokussierungsabhängigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung. Z. Naturforsch. 21a, 476-478 (1966).
30. van Heel, M., Harauz, G., Orlova, E. V., Schmidt, R. & Schatz, M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116, 17-24 (1996).
31. van Heel, M. et al. Single-particle electron cryo-microscopy: towards atomic resolution. Q. Rev. Biophys. 33, 307-369 (2000).
32. Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
33. Grigorieff, N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277, 1033-1046 (1998).
34. Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
35. Huang, C. C., Couch, G. S., Pettersen, E. F. & Ferrin, T. E. Chimera: an extensible molecular modeling application constructed using standard components. Pacif. Symp. Biocomput. 1, 724 (1996).
36. Jones, T. A., Zou, J.-Y. & Cowan, S. W. 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).
37. Jones, T. A. (ed.) A, yaap, asap, @#*? A Set of Averaging Programs (SERC Daresbury Laboratory, Warrington, 1992).
38. Kleywegt, G. J. & Jones, T. A. Software for handling macromolecular envelopes. Acta Crystallogr. D 55, 941-944 (1999).
39. Marti-Renom, M. A. et al. Comparative protein structure modeling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29, 291-325 (2000).
40. Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
41. Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).