Nuclear Lamina Interactions

Nuclear lamina interactions are the molecular contacts between the nuclear lamina, chromatin, and proteins of the inner nuclear membrane that organize the nucleus and support its mechanical stability. The lamina, composed mainly of lamin intermediate filaments, binds membrane-associated proteins and lamina-associated chromatin domains, influencing genome positioning, gene regulation, and responses to mechanical stress. These interactions change during development, differentiation, and cell-cycle progression, linking nuclear architecture to cellular function. Studying them helps explain how mutations in lamins and associated proteins cause laminopathies, while providing insight into genome organization, mechanotransduction, tissue development, and potential therapeutic strategies.

Nuclear Lamina Interactions - Related Videos

Research

JoVE Journal - Biochemistry

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

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2017

We have established a method for the purification of coregulatory interaction proteins using the LC-MS/MS system.

Education

JoVE Core - Chemistry

Nuclear Stability

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2020

Protons and neutrons, collectively called nucleons, are packed together tightly in a nucleus. With a radius of about 10−15 meters, a nucleus is quite small compared to the radius of the entire atom, which is about 10−10 meters. Nuclei are extremely dense compared to bulk matter, averaging 1.8 × 1014 grams per cubic centimeter. If the earth’s density were equal to the average nuclear density, the earth’s radius would be only about 200 meters. To hold positively charged protons together in the...

Nuclear Magnetic Resonance to Study Atomic Level Protein-Protein Interactions

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2025

This video describes the nuclear magnetic resonance spectroscopy technique to study protein-protein interactions between 15N-labeled wild-type and mutant envoplakin proteins and the unlabeled vimentin protein. The successful interaction between wild-type envoplakin and vimentin leads to extensive line broadening and peak disappearance in the NMR spectra, whereas the absence of an interaction between the mutated envoplakin and vimentin results in well-resolved peaks in the NMR spectra.

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

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2025

This NMR-based protocol investigates weak protein-glycan interactions using cyanovirin-N and D-mannose. Combining ligand- and protein-detected methods, it maps binding sites, detects allosteric effects, and identifies encounter complexes. The approach outlines sample preparation and data analysis, offering structural and dynamic insights valuable for glycan-specific diagnostics and recognition mechanisms.

Production of Synthetic Nuclear Melt Glass

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Cited by 1 •

2016

A protocol for the production of synthetic nuclear melt glass, similar to trinitite, is presented.

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