Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Dec;84(24):8805–8809. doi: 10.1073/pnas.84.24.8805

Clathrin heavy chain: molecular cloning and complete primary structure.

T Kirchhausen 1, S C Harrison 1, E P Chow 1, R J Mattaliano 1, K L Ramachandran 1, J Smart 1, J Brosius 1
PMCID: PMC299639  PMID: 3480512

Abstract

We have deduced the 1675-amino acid sequence of rat clathrin heavy chain from cDNA clones and predict a protein of Mr 191,569. We have established the polarity of the heavy chain and assigned sequence positions to several structural landmarks of the clathrin leg. The terminal domain at the distal end of the clathrin leg is at the amino terminus of the heavy chain. It is connected to the distal segment by a flexible "link" from Tyr-479 to Arg-523. There is an unusual sequence at the carboxyl terminus that may form the globular projection at the vertex of the clathrin trimer. We suggest that a possible site of heavy-chain-light-chain interaction is located in the proximal segment. Comparison with other partially sequenced mammalian clathrin heavy chains shows that the primary structure is highly conserved. The heavy chain is unrelated to other classes of structural proteins.

Full text

PDF
8805

Images in this article

8806Image
on p.8806
8808Image
on p.8808
8808Image
on p.8808

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 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]
  2. 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]
  3. Goldstein J. L., Anderson R. G., Brown M. S. Coated pits, coated vesicles, and receptor-mediated endocytosis. Nature. 1979 Jun 21;279(5715):679–685. doi: 10.1038/279679a0. [DOI] [PubMed] [Google Scholar]
  4. Harrison S. C., Kirchhausen T. Clathrin, cages, and coated vesicles. Cell. 1983 Jul;33(3):650–652. doi: 10.1016/0092-8674(83)90007-7. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Hogle J. M., Chow M., Filman D. J. Three-dimensional structure of poliovirus at 2.9 A resolution. Science. 1985 Sep 27;229(4720):1358–1365. doi: 10.1126/science.2994218. [DOI] [PubMed] [Google Scholar]
  7. Hunkapiller M. W., Lujan E., Ostrander F., Hood L. E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 1983;91:227–236. doi: 10.1016/s0076-6879(83)91019-4. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. Kirchhausen T., Harrison S. C., Heuser J. Configuration of clathrin trimers: evidence from electron microscopy. J Ultrastruct Mol Struct Res. 1986 Mar;94(3):199–208. doi: 10.1016/0889-1605(86)90067-4. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. Kozak M. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res. 1981 Oct 24;9(20):5233–5252. doi: 10.1093/nar/9.20.5233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  17. Maizel J. V., Jr, Lenk R. P. Enhanced graphic matrix analysis of nucleic acid and protein sequences. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7665–7669. doi: 10.1073/pnas.78.12.7665. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Maruyama T., Gojobori T., Aota S., Ikemura T. Codon usage tabulated from the GenBank genetic sequence data. Nucleic Acids Res. 1986;14 (Suppl):r151–r197. doi: 10.1093/nar/14.suppl.r151. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  20. McLachlan A. D., Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature. 1982 Sep 16;299(5880):226–231. doi: 10.1038/299226a0. [DOI] [PubMed] [Google Scholar]
  21. McLachlan A. D., Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J Mol Biol. 1983 Mar 15;164(4):605–626. doi: 10.1016/0022-2836(83)90053-0. [DOI] [PubMed] [Google Scholar]
  22. Mocchetti I., Einstein R., Brosius J. Putative diazepam binding inhibitor peptide: cDNA clones from rat. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7221–7225. doi: 10.1073/pnas.83.19.7221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Oliver D. B., Crowther R. A. DNA sequence of the tail fibre genes 36 and 37 of bacteriophage T4. J Mol Biol. 1981 Dec 15;153(3):545–568. doi: 10.1016/0022-2836(81)90407-1. [DOI] [PubMed] [Google Scholar]
  24. Payne G. S., Schekman R. A test of clathrin function in protein secretion and cell growth. Science. 1985 Nov 29;230(4729):1009–1014. doi: 10.1126/science.2865811. [DOI] [PubMed] [Google Scholar]
  25. Pearse B. M. Coated vesicles from pig brain: purification and biochemical characterization. J Mol Biol. 1975 Sep 5;97(1):93–98. doi: 10.1016/s0022-2836(75)80024-6. [DOI] [PubMed] [Google Scholar]
  26. Pretorius H. T., Nandi P. K., Lippoldt R. E., Johnson M. L., Keen J. H., Pastan I., Edelhoch H. Molecular characterization of human clathrin. Biochemistry. 1981 May 12;20(10):2777–2782. doi: 10.1021/bi00513a011. [DOI] [PubMed] [Google Scholar]
  27. Reed K. C., Mann D. A. Rapid transfer of DNA from agarose gels to nylon membranes. Nucleic Acids Res. 1985 Oct 25;13(20):7207–7221. doi: 10.1093/nar/13.20.7207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. 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]
  29. Ullrich A., Berman C. H., Dull T. J., Gray A., Lee J. M. Isolation of the human insulin-like growth factor I gene using a single synthetic DNA probe. EMBO J. 1984 Feb;3(2):361–364. doi: 10.1002/j.1460-2075.1984.tb01812.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. 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]
  31. 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]
  32. 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]
  33. 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]
  34. Wallner B. P., Mattaliano R. J., Hession C., Cate R. L., Tizard R., Sinclair L. K., Foeller C., Chow E. P., Browing J. L., Ramachandran K. L. Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity. Nature. 1986 Mar 6;320(6057):77–81. doi: 10.1038/320077a0. [DOI] [PubMed] [Google Scholar]
  35. 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]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES