Cited by 146Nuclear Structure and FunctionGenomics and Chromatin DynamicsSkin and Cellular Biology Research

Detergent–salt resistance of LAP2α in interphase nuclei and phosphorylation‐dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics

Open access
Dechat, Thomas, Gotzmann, Josef, Stockinger, Andreas, Harris, Crafford A., Ann Talle, Mary, Siekierka, John J., Foisner, Roland·1998·The EMBO Journal

Abstract

Lamina-associated polypeptide (LAP) 2 of the inner nuclear membrane (now LAP2beta) and LAP2alpha are related proteins produced by alternative splicing, and contain a common 187 amino acid N-terminal domain. We show here that, unlike LAP2beta, LAP2alpha behaved like a nuclear non-membrane protein in subcellular fractionation studies and was localized throughout the nuclear interior in interphase cells. It co-fractionated with LAP2beta in nuclear lamina/matrix-enriched fractions upon extraction of nuclei with detergent, salt and nucleases. During metaphase LAP2alpha dissociated from chromosomes and became concentrated around the spindle poles. Furthermore, LAP2alpha was mitotically phosphorylated, and phosphorylation correlated with increased LAP2alpha solubility upon extraction of cells in physiological buffers. LAP2alpha relocated to distinct sites around chromosomes at early stages of nuclear reassembly and intermediarily co-localized with peripheral lamin B and intranuclear lamin A structures at telophase. During in vitro nuclear assembly LAP2alpha was dephosphorylated and assembled into insoluble chromatin-associated structures, and recombinant LAP2alpha was found to interact with chromosomes in vitro. Some LAP2alpha may also associate with membranes prior to chromatin attachment. Altogether the data suggest a role of LAP2alpha in post-mitotic nuclear assembly and in the dynamic structural organization of the nucleus.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1093/emboj/17.16.4887

Cites

76 of 76 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • LAP2α is localized throughout the nuclear interior and is implicated in the structural organization of the nucleus.

    “while LAP2α is localized throughout the nuclear interior and is implicated in the structural organization of the nucleus (Dechat et al., 1998).”

    From Impact of Alternative Splicing on the Human Proteome (2017) · cites this paper as Dechat et al., 1998

  • LAP2β localizes to the nuclear lamina and represses transcription of p53 and NF-κB target genes.

    “LAP2β localizes to the nuclear lamina and represses transcription of p53 and nuclear factor κB (NF-κB) target genes (Dechat et al., 1998, Somech et al., 2005)”

    From Impact of Alternative Splicing on the Human Proteome (2017) · cites this paper as Dechat et al., 1998

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Dechat, T., Gotzmann, J., Stockinger, A., Harris, C. A., Ann Talle, M., Siekierka, J. J., & Foisner, R.
Affiliations
University of Vienna (AT)
Corresponding author
Foisner, Roland
Venue
The EMBO Journal
Published
1998-08-17
Volume
17
Issue
16
Pages
4887-4902
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W2102613320
Cited by
146
References
76
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 5 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 2 · 2013: 3 · 2012: 5
FWCI
4.54
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Austrian Science Fund
  • Universität Wien
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Keywords
LAP2α, inner nuclear membrane, nuclear lamina, nuclear assembly, mitotic phosphorylation, nuclear lamins, chromosome association, interphase nuclei, alternative splicing, telophase, chromatin
MeSH terms
Animals, Cell Nucleus, Detergents, DNA-Binding Proteins, Cricetinae, HeLa Cells, Humans, Interphase, Membrane Proteins, Mitosis, Nuclear Proteins, Phosphorylation, Salts, Microscopy, Immunoelectron, CHO Cells

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review