Abstract
Two regions on the clathrin heavy chain that are involved in triskelion interactions during assembly have been localized on the triskelion structure. These regions were previously identified with anti-heavy chain monoclonal antibodies X19 and X35, which disrupt clathrin assembly (Blank, G. S., and F. M. Brodsky, 1986, EMBO (Eur. Mol. Biol. Organ.) J., 5:2087-2095). Antibody-binding sites were determined based on their reactivity with truncated triskelions, and were mapped to an 8- kD region in the middle of the proximal portion of the triskelion arm (X19) and a 6-kD region at the triskelion elbow (X35). The elbow site implicated in triskelion assembly was also shown to be included within a heavy chain region involved in binding the light chains and to constitute part of the light chain-binding site. We postulate that this region of the heavy chain binds to the interaction site identified on the light chains that has homology to intermediate filament proteins (Brodsky, F. M., C. J. Galloway, G. S. Blank, A. P. Jackson, H.-F. Seow, K. Drickamer, and P. Parham, 1987, Nature (Lond.), 326:203-205). These findings suggest the existence of a heavy chain site, near the triskelion elbow, which is involved in both intramolecular and intermolecular interactions during clathrin assembly.
Full Text
The Full Text of this article is available as a PDF (1.6 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bar-Zvi D., Branton D. Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II. J Biol Chem. 1986 Jul 25;261(21):9614–9621. [PubMed] [Google Scholar]
- Blank G. S., Brodsky F. M. Site-specific disruption of clathrin assembly produces novel structures. EMBO J. 1986 Sep;5(9):2087–2095. doi: 10.1002/j.1460-2075.1986.tb04470.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brodsky F. M. Clathrin structure characterized with monoclonal antibodies. I. Analysis of multiple antigenic sites. J Cell Biol. 1985 Dec;101(6):2047–2054. doi: 10.1083/jcb.101.6.2047. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brodsky F. M., Galloway C. J., Blank G. S., Jackson A. P., Seow H. F., Drickamer K., Parham P. Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity. Nature. 1987 Mar 12;326(6109):203–205. doi: 10.1038/326203a0. [DOI] [PubMed] [Google Scholar]
- Brodsky F. M., Holmes N. J., Parham P. Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification. J Cell Biol. 1983 Mar;96(3):911–914. doi: 10.1083/jcb.96.3.911. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brodsky F. M., Parham P. Polymorphism in clathrin light chains from different tissues. J Mol Biol. 1983 Jun 15;167(1):197–204. doi: 10.1016/s0022-2836(83)80041-2. [DOI] [PubMed] [Google Scholar]
- Chen Y. X., Evans R. L., Pollack M. S., Lanier L. L., Phillips J. H., Rousso C., Warner N. L., Brodsky F. M. Characterization and expression of the HLA-DC antigens defined by anti-Leu 10. Hum Immunol. 1984 Aug;10(4):221–235. doi: 10.1016/0198-8859(84)90088-0. [DOI] [PubMed] [Google Scholar]
- Crowther R. A., Finch J. T., Pearse B. M. On the structure of coated vesicles. J Mol Biol. 1976 Jun 5;103(4):785–798. doi: 10.1016/0022-2836(76)90209-6. [DOI] [PubMed] [Google Scholar]
- Crowther R. A., Pearse B. M. Assembly and packing of clathrin into coats. J Cell Biol. 1981 Dec;91(3 Pt 1):790–797. doi: 10.1083/jcb.91.3.790. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Geisler N., Fischer S., Vandekerckhove J., Plessmann U., Weber K. Hybrid character of a large neurofilament protein (NF-M): intermediate filament type sequence followed by a long and acidic carboxy-terminal extension. EMBO J. 1984 Nov;3(11):2701–2706. doi: 10.1002/j.1460-2075.1984.tb02196.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldstein J. L., Brown M. S., Anderson R. G., Russell D. W., Schneider W. J. Receptor-mediated endocytosis: concepts emerging from the LDL receptor system. Annu Rev Cell Biol. 1985;1:1–39. doi: 10.1146/annurev.cb.01.110185.000245. [DOI] [PubMed] [Google Scholar]
- Heuser J., Kirchhausen T. Deep-etch views of clathrin assemblies. J Ultrastruct Res. 1985 Jul-Aug;92(1-2):1–27. doi: 10.1016/0889-1605(85)90123-5. [DOI] [PubMed] [Google Scholar]
- Heuser J. Three-dimensional visualization of coated vesicle formation in fibroblasts. J Cell Biol. 1980 Mar;84(3):560–583. doi: 10.1083/jcb.84.3.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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. 1987 Mar 12;326(6109):154–159. doi: 10.1038/326154a0. [DOI] [PubMed] [Google Scholar]
- Kanaseki T., Kadota K. The "vesicle in a basket". A morphological study of the coated vesicle isolated from the nerve endings of the guinea pig brain, with special reference to the mechanism of membrane movements. J Cell Biol. 1969 Jul;42(1):202–220. doi: 10.1083/jcb.42.1.202. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Keen J. H., Willingham M. C., Pastan I. H. Clathrin-coated vesicles: isolation, dissociation and factor-dependent reassociation of clathrin baskets. Cell. 1979 Feb;16(2):303–312. doi: 10.1016/0092-8674(79)90007-2. [DOI] [PubMed] [Google Scholar]
- Kirchhausen T., Harrison S. C., Parham P., Brodsky F. M. Location and distribution of the light chains in clathrin trimers. Proc Natl Acad Sci U S A. 1983 May;80(9):2481–2485. doi: 10.1073/pnas.80.9.2481. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kirchhausen T., Harrison S. C. Protein organization in clathrin trimers. Cell. 1981 Mar;23(3):755–761. doi: 10.1016/0092-8674(81)90439-6. [DOI] [PubMed] [Google Scholar]
- Kirchhausen T., Harrison S. C. Structural domains of clathrin heavy chains. J Cell Biol. 1984 Nov;99(5):1725–1734. doi: 10.1083/jcb.99.5.1725. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kirchhausen T., Scarmato P., Harrison S. C., Monroe J. J., Chow E. P., Mattaliano R. J., Ramachandran K. L., Smart J. E., Ahn A. H., Brosius J. Clathrin light chains LCA and LCB are similar, polymorphic, and share repeated heptad motifs. Science. 1987 Apr 17;236(4799):320–324. doi: 10.1126/science.3563513. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Linden C. D. Identification of the coated vesicle proteins that bind calmodulin. Biochem Biophys Res Commun. 1982 Nov 16;109(1):186–193. doi: 10.1016/0006-291x(82)91583-2. [DOI] [PubMed] [Google Scholar]
- Lisanti M. P., Shapiro L. S., Moskowitz N., Hua E. L., Puszkin S., Schook W. Isolation and preliminary characterization of clathrin-associated proteins. Eur J Biochem. 1982 Jul;125(2):463–470. doi: 10.1111/j.1432-1033.1982.tb06706.x. [DOI] [PubMed] [Google Scholar]
- McKeon F. D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 1986 Feb 6;319(6053):463–468. doi: 10.1038/319463a0. [DOI] [PubMed] [Google Scholar]
- Mooibroek M. J., Michiel D. F., Wang J. H. Clathrin light chains are calcium-binding proteins. J Biol Chem. 1987 Jan 5;262(1):25–28. [PubMed] [Google Scholar]
- Nandi P. K., Pretorius H. T., Lippoldt R. E., Johnson M. L., Edelhoch H. Molecular properties of the reassembled coat protein of coated vesicles. Biochemistry. 1980 Dec 9;19(25):5917–5921. doi: 10.1021/bi00566a039. [DOI] [PubMed] [Google Scholar]
- Parham P., Androlewicz M. J., Brodsky F. M., Holmes N. J., Ways J. P. Monoclonal antibodies: purification, fragmentation and application to structural and functional studies of class I MHC antigens. J Immunol Methods. 1982 Sep 17;53(2):133–173. doi: 10.1016/0022-1759(82)90137-5. [DOI] [PubMed] [Google Scholar]
- Pearse B. M., Bretscher M. S. Membrane recycling by coated vesicles. Annu Rev Biochem. 1981;50:85–101. doi: 10.1146/annurev.bi.50.070181.000505. [DOI] [PubMed] [Google Scholar]
- Pearse B. M. On the structural and functional components of coated vesicles. J Mol Biol. 1978 Dec 25;126(4):803–812. doi: 10.1016/0022-2836(78)90021-9. [DOI] [PubMed] [Google Scholar]
- Pearse B. M., Robinson M. S. Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 1984 Sep;3(9):1951–1957. doi: 10.1002/j.1460-2075.1984.tb02075.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schmid S. L., Matsumoto A. K., Rothman J. E. A domain of clathrin that forms coats. Proc Natl Acad Sci U S A. 1982 Jan;79(1):91–95. doi: 10.1073/pnas.79.1.91. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schook W. J., Puszkin S. Brain clathrin light chain 2 can be phosphorylated by a coated vesicle kinase. Proc Natl Acad Sci U S A. 1985 Dec;82(23):8039–8043. doi: 10.1073/pnas.82.23.8039. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schook W., Puszkin S., Bloom W., Ores C., Kochwa S. Mechanochemical properties of brain clathrin: interactions with actin and alpha-actinin and polymerization into basketlike structures or filaments. Proc Natl Acad Sci U S A. 1979 Jan;76(1):116–120. doi: 10.1073/pnas.76.1.116. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sorger P. K., Crowther R. A., Finch J. T., Pearse B. M. Clathrin cubes: an extreme variant of the normal cage. J Cell Biol. 1986 Oct;103(4):1213–1219. doi: 10.1083/jcb.103.4.1213. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steinert P. M., Steven A. C., Roop D. R. The molecular biology of intermediate filaments. Cell. 1985 Sep;42(2):411–420. doi: 10.1016/0092-8674(85)90098-4. [DOI] [PubMed] [Google Scholar]
- Tyler J. M., Branton D. Rotary shadowing of extended molecules dried from glycerol. J Ultrastruct Res. 1980 May;71(2):95–102. doi: 10.1016/s0022-5320(80)90098-2. [DOI] [PubMed] [Google Scholar]
- Ungewickell E. Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. EMBO J. 1983;2(8):1401–1408. doi: 10.1002/j.1460-2075.1983.tb01598.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ungewickell E., Branton D. Assembly units of clathrin coats. Nature. 1981 Jan 29;289(5796):420–422. doi: 10.1038/289420a0. [DOI] [PubMed] [Google Scholar]
- Ungewickell E., Unanue E. R., Branton D. Functional and structural studies on clathrin triskelions and baskets. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):723–731. doi: 10.1101/sqb.1982.046.01.069. [DOI] [PubMed] [Google Scholar]
- Usami M., Takahashi A., Kadota T., Katoda K. Phosphorylation of a clathrin light chain of coated vesicles in the presence of histones. J Biochem. 1985 Jun;97(6):1819–1822. doi: 10.1093/oxfordjournals.jbchem.a135243. [DOI] [PubMed] [Google Scholar]
- Vigers G. P., Crowther R. A., Pearse B. M. Three-dimensional structure of clathrin cages in ice. EMBO J. 1986 Mar;5(3):529–534. doi: 10.1002/j.1460-2075.1986.tb04242.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Winkler F. K., Stanley K. K. Clathrin heavy chain, light chain interactions. EMBO J. 1983;2(8):1393–1400. doi: 10.1002/j.1460-2075.1983.tb01597.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woodward M. P., Roth T. F. Coated vesicles: characterization, selective dissociation, and reassembly. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4394–4398. doi: 10.1073/pnas.75.9.4394. [DOI] [PMC free article] [PubMed] [Google Scholar]