ArticleMolecular and cellular biochemistry2015
LAP1 is a crucial protein for the maintenance of the nuclear envelope structure and cell cycle progression.
Article in Molecular and cellular biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- TOR1 AIP1 interacts with p53 to enhance cell cycle dysregulation in prostate cancer progression.Molecular and cellular biochemistry · 2025Article
- LAP1 Interactome Profiling Provides New Insights into LAP1's Physiological Functions.International journal of molecular sciences · 2024Article
- Quantitative proteome analysis of LAP1-deficient human fibroblasts: A pilot approach for predicting the signaling pathways deregulated in LAP1-associated diseases.Biochemistry and biophysics reports · 2024Article
- Review
- Loss of the Nuclear Envelope Protein LAP1B Disrupts the Myogenic Differentiation of Patient-Derived Fibroblasts.International journal of molecular sciences · 2022Article
- Nuclear Envelope Alterations in Myotonic Dystrophy Type 1 Patient-Derived Fibroblasts.International journal of molecular sciences · 2022Article
- Review
- Article
- Nuclear Accumulation of LAP1:TRF2 Complex during DNA Damage Response Uncovers a Novel Role for LAP1.Cells · 2020Article
- Article
- DYT1 Dystonia Patient-Derived Fibroblasts Have Increased Deformability and Susceptibility to Damage by Mechanical Forces.Frontiers in cell and developmental biology · 2019Article
- Descriptive Analysis of LAP1 Distribution and That of Associated Proteins throughout Spermatogenesis.Membranes · 2017Article
- Article
- Identification of a novel human LAP1 isoform that is regulated by protein phosphorylation.PloS one · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell division in eukaryotes requires the disassembly of the nuclear envelope (NE) at the beginning of mitosis and its reassembly at the end of mitosis. These processes are complex and involve coordinated steps where NE proteins have a crucial role. Lamina-associated polypeptide 1 (LAP1) is an inner nuclear membrane protein that has been associated with cell cycle events. In support of this role, LAP1 has been implicated in the regulation of the NE reassembly and assembly of the mitotic spindle during mitosis. In this study, we demonstrated that LAP1 intracellular levels vary during the cell cycle in SH-SY5Y cells, and that LAP1 is highly phosphorylated during mitosis. It is also clear that LAP1 co-localized with acetylated α-tubulin in the mitotic spindle and with γ-tubulin in centrosomes (main microtubule organizing center) in mitotic cells. Moreover, LAP1 knockdown resulted in decreased number of mitotic cells and decreased levels of acetylated α-tubulin (marker of microtubules stability) and lamin B1. Additionally, it was possible to determine that LAP1 is important for centrosome positioning near the NE. These findings place LAP1 at a key position to participate in the maintenance of the NE structure and progression of the cell cycle.
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