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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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...

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Related Experiment Video

Updated: Jun 23, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
10:12

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

Shining a light on post-translational modification.

Nigel G J Richards1

  • 1Department of Chemistry, P.O. Box 117200, University of Florida, Gainesville, FL 32611-7200, USA.

HFSP Journal
|May 1, 2009
PubMed
Summary
This summary is machine-generated.

Researchers can now control protein modifications and movement using photocaged proteins. This technique helps understand protein function timing and organelle targeting, advancing biological research.

More Related Videos

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Related Experiment Videos

Last Updated: Jun 23, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
10:12

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology

Background:

  • Post-translational modifications (PTMs) like phosphorylation and glycosylation diversify protein structures and regulate cellular functions.
  • Aberrant PTMs and protein mislocalization are linked to various diseases.
  • Traditional mutagenesis methods for studying PTMs often only reveal 'loss of function' effects.

Purpose of the Study:

  • To introduce a novel method for investigating the dynamic roles of PTMs in cellular processes.
  • To address limitations of traditional mutagenesis in studying PTM timing and protein trafficking.
  • To explore the functional significance of precise temporal control over PTMs.

Main Methods:

  • Utilizing genetically encoded "photocaged" proteins.
  • Combining chemical synthesis with biological protein synthesis machinery.
  • Employing site-specific photocleavage to control PTM events in real-time.

Main Results:

  • Demonstrated the successful application of photocaged proteins to study PTM dynamics.
  • Provided a method to resolve questions about the timing of PTMs and protein localization.
  • Showcased the potential for precise temporal control over protein modifications.

Conclusions:

  • Photocaged proteins offer an advanced tool for dissecting the functional importance of PTM timing and localization.
  • This approach enhances our understanding of how dynamic PTMs influence cellular function and disease.
  • The integration of chemical and biological methods opens new avenues in protein research.