Three-dimensional structure of clathrin cages in ice - PubMed (original) (raw)
Three-dimensional structure of clathrin cages in ice
G P Vigers et al. EMBO J. 1986 Mar.
Abstract
We have collected tilt series of electron micrographs from unstained clathrin cages embedded in vitreous ice. From these micrographs we have generated three-dimensional reconstructions of individual hexagonal barrels, which show details of the internal structure. Four types of preparation have been examined: (i) coated vesicles; (ii) cages reassembled from clathrin heavy and light chains; (iii) reassembled cages treated with elastase to remove the light chains; and (iv) reassembled cages treated with trypsin to remove the light chains and the terminal domains of the clathrin heavy chains. In the intact and elastase-treated cages, the clathrin extends from the vertices into the interior of the polyhedron and forms an inner shell of material. Limited digestion with trypsin removes the inner shell, which indicates that this material corresponds to the terminal domains of the clathrin heavy chains.
Similar articles
- Location of the 100 kd-50 kd accessory proteins in clathrin coats.
Vigers GP, Crowther RA, Pearse BM. Vigers GP, et al. EMBO J. 1986 Sep;5(9):2079-85. doi: 10.1002/j.1460-2075.1986.tb04469.x. EMBO J. 1986. PMID: 2877872 Free PMC article. - Structural domains of clathrin heavy chains.
Kirchhausen T, Harrison SC. Kirchhausen T, et al. J Cell Biol. 1984 Nov;99(5):1725-34. doi: 10.1083/jcb.99.5.1725. J Cell Biol. 1984. PMID: 6386825 Free PMC article. - Protein organization in clathrin trimers.
Kirchhausen T, Harrison SC. Kirchhausen T, et al. Cell. 1981 Mar;23(3):755-61. doi: 10.1016/0092-8674(81)90439-6. Cell. 1981. PMID: 7226229 - The association of clathrin fragments with coated vesicle membranes.
Hanspal M, Luna E, Branton D. Hanspal M, et al. J Biol Chem. 1984 Sep 10;259(17):11075-82. J Biol Chem. 1984. PMID: 6147350 - Clathrin: anatomy of a coat protein.
Smith CJ, Pearse BM. Smith CJ, et al. Trends Cell Biol. 1999 Sep;9(9):335-8. doi: 10.1016/s0962-8924(99)01631-1. Trends Cell Biol. 1999. PMID: 10461185 Review.
Cited by
- A balance between membrane elasticity and polymerization energy sets the shape of spherical clathrin coats.
Saleem M, Morlot S, Hohendahl A, Manzi J, Lenz M, Roux A. Saleem M, et al. Nat Commun. 2015 Feb 19;6:6249. doi: 10.1038/ncomms7249. Nat Commun. 2015. PMID: 25695735 Free PMC article. - Three-dimensional image reconstruction of insect flight muscle. I. The rigor myac layer.
Taylor KA, Reedy MC, Córdova L, Reedy MK. Taylor KA, et al. J Cell Biol. 1989 Sep;109(3):1085-102. doi: 10.1083/jcb.109.3.1085. J Cell Biol. 1989. PMID: 2768334 Free PMC article. - Location of the 100 kd-50 kd accessory proteins in clathrin coats.
Vigers GP, Crowther RA, Pearse BM. Vigers GP, et al. EMBO J. 1986 Sep;5(9):2079-85. doi: 10.1002/j.1460-2075.1986.tb04469.x. EMBO J. 1986. PMID: 2877872 Free PMC article. - Genetic analysis of clathrin function in yeast.
Payne GS. Payne GS. J Membr Biol. 1990 Jun;116(2):93-105. doi: 10.1007/BF01868668. J Membr Biol. 1990. PMID: 2199679 Review. - Adaptor complex-independent clathrin function in yeast.
Yeung BG, Phan HL, Payne GS. Yeung BG, et al. Mol Biol Cell. 1999 Nov;10(11):3643-59. doi: 10.1091/mbc.10.11.3643. Mol Biol Cell. 1999. PMID: 10564262 Free PMC article.
References
- Proc Natl Acad Sci U S A. 1982 Jan;79(1):91-5 - PubMed
- Annu Rev Biochem. 1981;50:85-101 - PubMed
- J Cell Biol. 1981 Dec;91(3 Pt 1):790-7 - PubMed
- Proc Natl Acad Sci U S A. 1982 Jan;79(2):451-5 - PubMed
- Cold Spring Harb Symp Quant Biol. 1982;46 Pt 2:723-31 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources