• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. Jun 1988; 85(12): 4325–4329.
PMCID: PMC280421

Heterotypic and homotypic associations between the nuclear lamins: site-specificity and control by phosphorylation.

Abstract

Using purified components in affinity chromatography and blot binding assays, we have found that rat liver lamins A, B, and C can associate in homotypic and heterotypic fashions. Heterotypic A-B and C-B complexes are unusually stable and involve the common amino-terminal domain of lamins A and C, but not their helical "rod" domain. A synthetic peptide, comprising the first 32 amino acid residues of lamins A and C, is able to fully compete with the intact molecules for binding to lamin B. Conversely, heterotypic A-C associations and homotypic A-A and C-C interactions appear significantly weaker than A/C-B binding and do not involve the lamin A and C amino-terminal domain. Homotypic B-B complexes are not formed to any considerable extent unless isolated lamin B subunits are "superphosphorylated" in vitro with protein kinase A. However, when lamins A and C are similarly modified, no changes in their binding specificity can be detected. These data suggest that the nuclear lamina, unlike other multicomponent intermediate filaments, constitutes a nonobligatory heteropolymer. They also indicate that cAMP-dependent phosphorylation of interphase lamin B could cause remodeling of the lamina and establishment of homopolymeric domains.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.2M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Franke WW, Scheer U, Krohne G, Jarasch ED. The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol. 1981 Dec;91(3 Pt 2):39s–50s. [PMC free article] [PubMed]
  • Burke B, Gerace L. A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell. 1986 Feb 28;44(4):639–652. [PubMed]
  • Newport J. Nuclear reconstitution in vitro: stages of assembly around protein-free DNA. Cell. 1987 Jan 30;48(2):205–217. [PubMed]
  • Georgatos SD, Blobel G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J Cell Biol. 1987 Jul;105(1):117–125. [PMC free article] [PubMed]
  • Georgatos SD, Weber K, Geisler N, Blobel G. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6780–6784. [PMC free article] [PubMed]
  • Aaronson RP, Blobel G. Isolation of nuclear pore complexes in association with a lamina. Proc Natl Acad Sci U S A. 1975 Mar;72(3):1007–1011. [PMC free article] [PubMed]
  • Benavente R, Krohne G, Franke WW. Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis. Cell. 1985 May;41(1):177–190. [PubMed]
  • Krohne G, Dabauvalle MC, Franke WW. Cell type-specific differences in protein composition of nuclear pore complex-lamina structures in oocytes and erythrocytes of Xenopus laevis. J Mol Biol. 1981 Sep 5;151(1):121–141. [PubMed]
  • McKeon FD, Kirschner MW, Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 1986 Feb 6;319(6053):463–468. [PubMed]
  • Fisher DZ, Chaudhary N, Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6450–6454. [PMC free article] [PubMed]
  • Aebi U, Cohn J, Buhle L, Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 1986 Oct 9;323(6088):560–564. [PubMed]
  • Gerace L, Blobel G. Nuclear lamina and the structural organization of the nuclear envelope. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):967–978. [PubMed]
  • Krohne G, Wolin SL, McKeon FD, Franke WW, Kirschner MW. Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. EMBO J. 1987 Dec 1;6(12):3801–3808. [PMC free article] [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed]
  • Franke WW, Schiller DL, Hatzfeld M, Winter S. Protein complexes of intermediate-sized filaments: melting of cytokeratin complexes in urea reveals different polypeptide separation characteristics. Proc Natl Acad Sci U S A. 1983 Dec;80(23):7113–7117. [PMC free article] [PubMed]
  • Stewart C, Burke B. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Cell. 1987 Nov 6;51(3):383–392. [PubMed]
  • Inagaki M, Nishi Y, Nishizawa K, Matsuyama M, Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature. 1987 Aug 13;328(6131):649–652. [PubMed]
  • O'Connor CM, Gard DL, Lazarides E. Phosphorylation of intermediate filament proteins by cAMP-dependent protein kinases. Cell. 1981 Jan;23(1):135–143. [PubMed]
  • Geisler N, Weber K. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. EMBO J. 1988 Jan;7(1):15–20. [PMC free article] [PubMed]

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

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

  • Compound
    Compound
    PubChem Compound links
  • MedGen
    MedGen
    Related information in MedGen
  • PubMed
    PubMed
    PubMed citations for these articles
  • Substance
    Substance
    PubChem Substance links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...