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Published on: January 17, 2025
Nuclear structures surrounding internal lamin invaginations
Soňa Legartová1, Lenka Stixová, Oskar Laur
1Institute of Biophysics, Academy of Sciences of the Czech Republic, 612 65, Brno, Czech Republic.
Insights
Nuclear lamins form internal channels that transport molecules within the cell nucleus. These channels interact with key nuclear structures, suggesting a role in cellular processes and nuclear architecture.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- A- and C-type lamins are intermediate filament proteins crucial for nuclear shape and architecture.
- Their precise function within the nuclear interior remains incompletely understood.
Purpose of the Study:
- To investigate the potential role of A/C-type lamin invaginations as channels for molecular transport.
- To identify nuclear components interacting with these proposed lamin channels.
Main Methods:
- Fluorescent protein technology for visualizing lamin structures.
- Immunofluorescence staining to detect interactions with nuclear and nucleolar components.
- Analysis of lamin distribution in various cell types.
Main Results:
- A/C-type lamin invaginations form channels within the nuclear interior.
- These channels associate with nucleoli, heterochromatin, polycomb group bodies, and DNA repair regions.
- Interactions were also observed with nuclear pores, LAP2α, and PML bodies.
- Inverse correlation between A/C-type and B-type lamins in specific regions.
Conclusions:
- Internal channels formed by A/C-type lamins likely facilitate the transport of regulatory molecules.
- These lamin channels play a role in organizing nuclear architecture and associating with diverse nuclear structures.
- Findings are consistent across various cell types, including stem cells.
Abstract:
A- and C-type lamins are intermediate filament proteins responsible for the maintenance of nuclear shape and most likely nuclear architecture. Here, we propose that pronounced invaginations of A/C-type lamins into the nuclear interior represent channels for the transport of regulatory molecules to and from nuclear and nucleolar regions. Using fluorescent protein technology and immunofluorescence, we show that A-type lamin channels interact with several nuclear components, including fibrillarin- and UBF-positive regions of nucleoli, foci of heterochromatin protein 1 β, polycomb group bodies, and genomic regions associated with DNA repair. Similar associations were observed between A/C-type lamin channels and nuclear pores, lamin-associated protein LAP2α, and promyelocytic leukemia nuclear bodies. Interestingly, regions with high levels of A/C-type lamins had low levels of B-type lamins, and vice versa. These characteristics were observed in primary and immortalized mouse embryonic fibroblasts as well as human and mouse embryonic stem cell colonies exhibiting stem cell-specific lamin positivity. Our findings indicate that internal channels formed by nuclear lamins likely contribute to normal cellular processes through association with various nuclear and nucleolar structures.
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