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

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
Labeling DNA Probes03:31

Labeling DNA Probes

8.1K
DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
8.1K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.6K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
6.6K

You might also read

Related Articles

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

Sort by
Same author

Concise Synthesis of (±)-Stephadiamine via Vinylogous Wenker Cyclization.

Journal of the American Chemical Society·2026
Same author

Protecting Groups as Dispersive Directing Groups: Toward the Asymmetric Synthesis of Altemicidin.

Organic letters·2026
Same author

An Agonist/Antagonist Photo-Switchable Vitamin D Mimetic Enables Bidirectional Optical Control of VDR.

Angewandte Chemie (International ed. in English)·2026
Same author

Metal-Dependent Photodissociation of Hydrazone Photoswitches from Rare-Earth Complexes.

Journal of the American Chemical Society·2026
Same author

The photodynamic inactivation in the control of the seafood zoonotic parasite, Anisakis sp.

Parasitology research·2026
Same author

Correction to "Synthesis of Collinoketones via Biomimetic [6 + 4] Cycloaddition".

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: Jun 12, 2025

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
10:49

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

12.6K

Light-Activatable, Cell-Type Specific Labeling of the Nascent Proteome.

H T Evans1, T Ko2, M M Oliveira1

  • 1Center for Neural Science, New York University, New York, New York 10003, United States.

ACS Chemical Neuroscience
|September 23, 2024
PubMed
Summary

Researchers developed Opto-ANL, a light-inducible method to precisely label newly synthesized proteins in specific cell types. This technique offers improved temporal control and efficiency for studying protein synthesis in neuroscience and other complex biological processes.

Keywords:
cell-type specificde novo proteomelight-induciblemRNA translationphotocagephotopharmacology

More Related Videos

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.4K
Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level
08:29

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

6.1K

Related Experiment Videos

Last Updated: Jun 12, 2025

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
10:49

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

12.6K
Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.4K
Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level
08:29

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

6.1K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Understanding protein synthesis is crucial for complex biological processes, especially in neuroscience for functions like memory formation.
  • Existing methods for labeling newly synthesized proteins lack the spatial and temporal resolution needed to study cell-type-specific translation.
  • Distinguishing overlapping periods of mRNA translation in different cell types remains a significant challenge.

Purpose of the Study:

  • To develop a novel, light-inducible method for precisely labeling newly synthesized proteins within targeted cell types.
  • To overcome the limitations of current techniques in achieving high spatial and temporal resolution for proteomic studies.
  • To enable detailed investigation of cell-type-specific protein synthesis during complex neurological functions.

Main Methods:

  • Development of Opto-ANL, a photocaged azidonorleucine (ANL) analog.
  • Utilizing a mutant methionyl-tRNA synthetase (L274G-MetRS) for targeted expression and ANL incorporation.
  • Employing UV light to uncage Opto-ANL, enabling visualization of newly synthesized proteins via fluorescent tagging.
  • Application in cell culture and mouse brain slices, including detection of insulin-induced protein synthesis.

Main Results:

  • Opto-ANL can be rapidly uncaged by UV light in both cell culture and brain slices.
  • Opto-ANL labeling allows for tight temporal control over the period of de novo proteomic labeling.
  • Labeling efficiency is improved with Opto-ANL compared to standard ANL.
  • Demonstrated application in detecting insulin-induced protein synthesis and labeling excitatory neuronal proteomes.

Conclusions:

  • Opto-ANL provides a powerful new tool for cell-type-specific, light-inducible proteomic labeling.
  • This photopharmacological approach enhances the ability to study dynamic changes in protein synthesis.
  • Enables novel insights into the role of the translational landscape in neurological phenomena like memory formation.