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Protein Signal Transduction in the Nucleus

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 May 2025 | Viewed by 959

Special Issue Editor


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Guest Editor
Department of Bioresources Engineering, Sejong University, Seoul 05006, Republic of Korea
Interests: signaling pathways; intranuclear; protein

Special Issue Information

Dear Colleagues,

The proteins in the nuclear membrane network not only maintain cell structure, but also regulate specific signal transduction in response to external stimuli. They can interact with signal proteins or transcription factors that enter the nucleus to regulate various life processes. These proteins function as signal regulators. This Special Issue focuses on the network of nuclear inner membrane proteins sharing the LAP2-emerin-MAN1-domain (LEM-D) and nuclear lamina, which are essential for maintaining the cell nuclear structure. The goal is to highlight their potential as significant signal transduction regulators. Research submissions on the interaction between other nuclear membrane proteins and signal-related factors within the nucleus are also welcome. Comprehensive studies of these proteins can help in the prevention of muscle diseases and cancer caused by signal regulation failure and contribute to the search for therapeutic targets for various diseases. This Special Issue aims to present a new paradigm that expands the field of intracellular signal regulation research into the nucleus, and shares systematic research approaches and results at a time when relevant research is increasing.

Dr. Jaekyung Shim
Guest Editor

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Keywords

  • inner nuclear membrane protein
  • protein network
  • LEM-domain proteins
  • nuclear lamina
  • signal transcription
  • transcriptional regulation

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Published Papers (1 paper)

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12 pages, 3194 KiB  
Case Report
Imaging-Based Molecular Interaction Between Src and Lamin A/C Mechanosensitive Proteins in the Nucleus of Laminopathic Cells
by Stefania Petrini, Giulia Bagnato, Michela Piccione, Valentina D’Oria, Valentina Apollonio, Marco Cappa, Claudia Castiglioni, Filippo Maria Santorelli, Teresa Rizza, Rosalba Carrozzo, Enrico Silvio Bertini and Barbara Peruzzi
Int. J. Mol. Sci. 2024, 25(24), 13365; https://doi.org/10.3390/ijms252413365 - 13 Dec 2024
Viewed by 663
Abstract
Laminopathies represent a wide range of genetic disorders caused by mutations in gene-encoding proteins of the nuclear lamina. Altered nuclear mechanics have been associated with laminopathies, given the key role of nuclear lamins as mechanosensitive proteins involved in the mechanotransduction process. To shed [...] Read more.
Laminopathies represent a wide range of genetic disorders caused by mutations in gene-encoding proteins of the nuclear lamina. Altered nuclear mechanics have been associated with laminopathies, given the key role of nuclear lamins as mechanosensitive proteins involved in the mechanotransduction process. To shed light on the nuclear partners cooperating with altered lamins, we focused on Src tyrosine kinase, known to phosphorylate proteins of the nuclear lamina. Here, we demonstrated a tight relationship between lamin A/C and Src in skin fibroblasts from two laminopathic patients, assessed by advanced imaging-based microscopy techniques. With confocal laser scanning and Stimulated Emission Depletion (STED) microscopy, a statistically significant higher co-distribution between the two proteins was observed in patients’ fibroblasts. Furthermore, the time-domain fluorescence lifetime imaging microscopy, combined with Förster resonance energy transfer detection, demonstrated a decreased lifetime value of Src (as donor fluorophore) in the presence of lamin A/C (as acceptor dye) in double-stained fibroblast nuclei in both healthy cells and patients’ cells, thereby indicating a molecular interaction that resulted significantly higher in laminopathic cells. All these results demonstrate a molecular interaction between Src and lamin A/C in healthy fibroblasts and their aberrant interaction in laminopathic nuclei, thus creating the possibilities of new diagnostic and therapeutic approaches for patients. Full article
(This article belongs to the Special Issue Protein Signal Transduction in the Nucleus)
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