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The nuclear lamina is a meshwork of intermediate-type filaments

The nuclear lamina is a meshwork of intermediate-type filaments The nuclear lamina, a protein meshwork lining the nucleoplasmic surface of the inner nuclear membrane1,2, is thought to provide a framework for organizing nuclear envelope structure3 and an anchoring site at the nuclear periphery for interphase chromatin3–5. In several higher eukaryotic cells, the lamina appears to be a polymer comprised mainly of one to three immunologically related polypeptides of relative molecular mass (M r) 60,000–75,000 (60–70K) termed lamins1,2. Three lamins (A, B, and C) are typically present in mammalian somatic cells. Previous studies on nuclear envelopes of rat liver6 and Xenopus oocytes7 suggested that the lamina has a fibrillar or filamentous substructure. Interestingly, protein sequences recently deduced for human lamins A and C from complementary DNA clones8,9 indicate that both of these polypeptides contain a region of ∼350 amino acids very similar in sequence to the coiled-coil α-helical rod domain that characterizes all intermediate-type filament (IF) proteins10,11. Here we analyse the supramolecular organization of the native nuclear lamina and the structure and assembly properties of purified lamins, and show that the lamins constitute a previously unrecognized class of IF polypeptides. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

The nuclear lamina is a meshwork of intermediate-type filaments

Aebi, Ueli; Cohn, Julie; Buhle, Loren; Gerace, Larry
Nature , Volume 323 (6088) – Oct 9, 1986
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References (31)

Publisher
Springer Journals
Copyright
Copyright © 1986 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/323560a0
Publisher site
See Article on Publisher Site

Abstract

The nuclear lamina, a protein meshwork lining the nucleoplasmic surface of the inner nuclear membrane1,2, is thought to provide a framework for organizing nuclear envelope structure3 and an anchoring site at the nuclear periphery for interphase chromatin3–5. In several higher eukaryotic cells, the lamina appears to be a polymer comprised mainly of one to three immunologically related polypeptides of relative molecular mass (M r) 60,000–75,000 (60–70K) termed lamins1,2. Three lamins (A, B, and C) are typically present in mammalian somatic cells. Previous studies on nuclear envelopes of rat liver6 and Xenopus oocytes7 suggested that the lamina has a fibrillar or filamentous substructure. Interestingly, protein sequences recently deduced for human lamins A and C from complementary DNA clones8,9 indicate that both of these polypeptides contain a region of ∼350 amino acids very similar in sequence to the coiled-coil α-helical rod domain that characterizes all intermediate-type filament (IF) proteins10,11. Here we analyse the supramolecular organization of the native nuclear lamina and the structure and assembly properties of purified lamins, and show that the lamins constitute a previously unrecognized class of IF polypeptides.

Journal

Nature – Springer Journals

Published: Oct 9, 1986

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