Related Experiment Video
Updated: Jul 2, 2025
16:43
Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
13.0K
Analyzing Photoactivation with Diffusion Models to Study Transport in the Endoplasmic Reticulum Network
Matteo Dora1, Frédéric Paquin-Lefebvre1, David Holcman1,2
1Applied Mathematics and Computational Biology, Ecole Normale Supérieure, Paris, France.
Methods in Molecular Biology (Clifton, N.J.)
|February 27, 2024
Summary
This study uses data-driven modeling to analyze photoactivation dynamics. It helps infer molecular propagation properties and cellular network motions from laser-induced fluorescence measurements.
Area of Science:
- Biophysics
- Cell Biology
- Computational Biology
Background:
- Photoactivation enables localized molecular fluorescence activation using laser illumination.
- Measuring molecular concentration changes between source and target regions is key.
- Understanding molecular propagation and cellular dynamics is crucial.
Purpose of the Study:
- To infer molecular propagation properties using data-driven modeling.
- To analyze cellular motions, like those in the endoplasmic reticulum, from photoactivation data.
- To extract biophysical parameters and reconstruct local network properties.
Main Methods:
- Reviewing data-driven analysis techniques.
- Employing diffusion-transport models.
- Utilizing numerical simulations for interpreting photoactivation dynamics.
Main Results:
- Interpreting photoactivation dynamics through data-driven models.
- Extracting essential biophysical parameters from experimental data.
- Reconstructing local network properties from photoactivation transients.
Conclusions:
- Data-driven modeling provides a robust framework for analyzing photoactivation.
- This approach allows for the inference of molecular propagation and cellular dynamics.
- Biophysical parameters and network properties can be effectively extracted.
More Related Videos
Related Concept Videos
01:27Post-translational Translocation of Proteins to the RER
5.7K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.7K
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
8.0K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
8.0K
01:24Protein Diffusion in the Membrane
4.4K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.4K
01:43The Endoplasmic Reticulum
13.6K
The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
13.6K
01:26Transport Across the Golgi
4.2K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
4.2K
01:44Introduction to Membrane Traffic
7.1K
The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
7.1K