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 accessAbstract
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.
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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
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- 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
- PMC
- PMC1170818
- 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
- bronze
- doi.org
- 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
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