Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

7.9K
Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
7.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.4K
Nuclear Export01:42

Nuclear Export

5.1K
The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
5.1K
Regulated mRNA Transport02:22

Regulated mRNA Transport

7.1K
In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
7.1K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

6.5K
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...
6.5K
Master Transcription Regulators02:23

Master Transcription Regulators

7.9K
Master transcription regulators are regulatory proteins that are predominantly responsible for regulating the expression of multiple genes. Often these genes work in concert to drive a  complex process. Activation of a master transcription regulator can lead to a cascade of transcriptional activation necessary for that outcome. These regulators can directly bind to the regulatory sequences of the various genes involved, or they can indirectly regulate transcription by binding to regulatory...
7.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Metabolic flexibility secures skeletal progenitor function upon reduced glycolysis driven by PFKFB3 loss.

Bone·2026
Same author

Correlating Stimulated Emission Depletion Microscopy With Fluorescence Lifetime Imaging Microscopy to Study the TIE2 Protein on Kidney Glomerular Podocytes.

The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society·2026
Same author

A novel model to study the impact of gender-affirming therapy on bone in young male mice.

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research·2026
Same author

R-loops as a trigger for intra- and extrachromosomal DNA amplification in cancer.

Frontiers in cell and developmental biology·2025
Same author

Cell-specific mRNA delivery via nanobody-functionalized lipid nanoparticles.

Journal of controlled release : official journal of the Controlled Release Society·2025
Same author

Microenvironment of Solid Tumors.

Frontiers in bioscience (Landmark edition)·2025

Related Experiment Video

Updated: Feb 24, 2026

Analysis of Spliceosomal snRNA Localization in Human Hela Cells Using Microinjection
07:35

Analysis of Spliceosomal snRNA Localization in Human Hela Cells Using Microinjection

Published on: August 6, 2019

6.5K

Two distinct nuclear localization signals in mammalian MSL1 regulate its function.

Ruslan I Dmitriev1, Nikolay B Pestov, Mikhail I Shakhparonov

  • 1School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10, Miklukho-Maklaya, 117997, Moscow, Russia.

Journal of Cellular Biochemistry
|June 11, 2014
PubMed
Summary

The MSL1 protein, interacting with KAT8, controls histone H4 acetylation. This study identifies two nuclear localization signals (NLS) in MSL1, influencing its function in stem and cancer cells.

Keywords:
HISTONE ACETYLATIONKAT8MSL1NUCLEUSSUB-NUCLEAR LOCALIZATION

More Related Videos

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.8K
Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

17.0K

Related Experiment Videos

Last Updated: Feb 24, 2026

Analysis of Spliceosomal snRNA Localization in Human Hela Cells Using Microinjection
07:35

Analysis of Spliceosomal snRNA Localization in Human Hela Cells Using Microinjection

Published on: August 6, 2019

6.5K
Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.8K
Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

17.0K

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cell Biology

Background:

  • The MSL1 protein's role in regulating histone H4 K16 acetylation is known, particularly its interaction with KAT8.
  • The functional significance of different mammalian MSL1 protein isoforms remains unclear.
  • Histone acetylation patterns are crucial for gene regulation in both normal stem cells and cancer cells.

Purpose of the Study:

  • To investigate the functional significance of mammalian MSL1 isoforms.
  • To identify and characterize nuclear localization signals (NLS) within the MSL1 protein.
  • To understand how MSL1 isoforms and their NLS influence histone acetylation and protein interactions.

Main Methods:

  • Bioinformatics analysis to identify potential NLS sequences.
  • Cellular localization studies using immunofluorescence.
  • Co-immunoprecipitation assays to study protein-protein interactions.
  • Western blotting to assess histone H4 K16 acetylation levels.

Main Results:

  • A novel nuclear localization signal (NLS) was identified in MSL1, in addition to a previously known bipartite NLS.
  • MSL1 isoforms possessing both NLS were found to localize to specific sub-nuclear foci.
  • These MSL1 isoforms target the co-chaperone protein TTC4 within these foci.
  • All identified MSL1 isoforms demonstrated the ability to affect histone H4 K16 acetylation.
  • The presence of two NLS in MSL1 facilitates the in vivo activity of KAT8.

Conclusions:

  • MSL1 protein isoforms possess distinct localization patterns mediated by two NLS.
  • MSL1's interaction with TTC4 and its role in H4K16 acetylation are linked to its nuclear localization.
  • The dual NLS system in MSL1 is critical for mediating KAT8 activity and global histone acetylation.
  • These findings provide insights into MSL1 function in stem and cancer cells.