Nuclear Proteins
Nuclear Proteins - Related Videos
10:03
Isolation of CA1 Nuclear Enriched Fractions from Hippocampal Slices to Study Activity-dependent Nuclear Import of Synapto-nuclear Messenger Proteins
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Cited by 8 •
2014
We provide a detailed protocol for induction of long-term potentiation in the CA1 region of the hippocampus and the subsequent isolation of nuclear enriched fractions from the tetanized area of the slice. This approach can be used to determine activity dependent nuclear protein import in cellular models of learning and memory.
05:43
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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Cited by 1 •
2017
We have established a method for the purification of coregulatory interaction proteins using the LC-MS/MS system.
01:34
Nuclear Protein Sorting
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2023
Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell. Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
06:05
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.
10:05
Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
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Cited by 15 •
2017
Protein-protein interactions can occur in both the nucleus and the cytoplasm of a cell. To investigate these interactions, traditional co-immunoprecipitation and modern proximity ligation assay are applied. In this study, we compare these two methods to visualize the distribution of NF90-RBM3 interactions in the nucleus and the cytoplasm.
FAQs
A nuclear localization signal acts as a recognition feature on a protein. Importin transport receptors bind this signal and carry the associated protein through a nuclear pore complex, the regulated gateway in the nuclear envelope. This mechanism helps concentrate appropriate proteins in the nucleus, where they can participate in genome-related activities rather than remaining distributed throughout the cell.
Interactions inside the nucleus depend on the protein’s molecular binding properties and the nuclear targets available to it. After import, a protein may associate with DNA, RNA, chromatin, or other nuclear factors. These distinct interactions place it in different regulatory contexts and allow nuclear proteins to influence gene activity, chromosome organization, or the processing of genetic information.
Some nuclear proteins remain in the nucleus and carry out sustained functions there, whereas others transit through the compartment as part of intracellular transport. This distinction helps researchers interpret localization correctly: nuclear presence does not by itself establish a permanent nuclear role. Determining how a protein behaves can clarify whether it directly supports genome activity or is being transported.
Defects can disrupt the processes that nuclear proteins support, including transcription, DNA replication, repair, RNA processing, and chromosome organization. Because these activities influence how genetic information is used, copied, maintained, and inherited, impaired protein function may alter cell growth or inheritance. Such defects are associated with developmental disorders, cancer, and other diseases.
Examining these proteins can show how molecular interactions within the nucleus control genome activity. Their associations with DNA, RNA, chromatin, and other nuclear factors provide connections between protein localization and the regulation of genetic information. This makes nuclear proteins useful for understanding how cells coordinate transcription and related nuclear processes during growth and inheritance.
Nuclear proteins contribute to chromosome organization, which helps maintain the arrangement and functional handling of genetic material in the nucleus. Their roles also connect nuclear activity with inheritance because DNA must be replicated, repaired, organized, and passed on accurately. Studying these relationships helps explain how cellular mechanisms support continuity of genetic information across cell growth and division.
Nuclear protein research is particularly relevant when abnormal nuclear transport or protein function is linked to developmental disorders, cancer, or other diseases. Investigators can examine how altered delivery into the nucleus, defective interactions, or impaired nuclear activities affect genome regulation. These connections help relate molecular mechanisms in the nucleus to broader changes in cell growth and function.