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Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins

Nature volume 319, pages 463–468 (1986)Cite this article

Abstract

The A, B and C lamins are the major proteins of the nuclear envelope. The complete nucleotide sequence of the coding region of the A and C lamins shows that these proteins are identical except for their carboxy termini. The most prominent structural feature of both lamins is an α-helical region of repeating heptads of amino acids that shows striking homology with the entire family of cytoplasmic intermediate filament proteins. These features suggest that the nuclear envelope is made up of a network of coiled-coil polymers.

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Author notes

  1. Daniel Caput

    Present address: ELF Biorecherche, La bege-innopole, BP 137 31328, Castanet Tolosan Cedex, France

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, 94143, USA

    Frank D. McKeon & Marc W. Kirschner

  2. Chiron Corporation, 4560 Horton St, Emeryville, California, 94608, USA

    Daniel Caput

Authors
  1. Frank D. McKeon
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  2. Marc W. Kirschner
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  3. Daniel Caput
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McKeon, F., Kirschner, M. & Caput, D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463–468 (1986). https://doi.org/10.1038/319463a0

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