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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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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...
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Endoplasmic Reticulum01:39

Endoplasmic Reticulum

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The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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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,...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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...
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Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

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Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
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Related Experiment Video

Updated: Aug 28, 2025

Author Spotlight: Regulation and Dysregulation of ER-Mitochondria Contacts — Implications for Neurodegenerative Disease Pathogenesis
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ER exit sites take the strain.

Maria Antonietta De Matteis1,2, Rossella Venditti1,2

  • 1Telethon Institute of Genetics and Medicine, Pozzuoli, Italy.

The EMBO Journal
|September 19, 2022
PubMed
Summary

Cellular growth adapts to mechanical strain through the heterodimerization of two small GTPases, as demonstrated by Phuyal et al. (2022). This molecular mechanism is key to understanding cellular mechanotransduction.

Area of Science:

  • Cell Biology
  • Mechanobiology
  • Molecular Cell Biology

Background:

  • Cells exhibit adaptive growth in response to external mechanical forces.
  • Cellular mechanical sensing is a fundamental biological process.
  • Small GTPases play crucial roles in cellular signaling pathways.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying cellular adaptation to mechanical strain.
  • To identify key proteins involved in mechanotransduction.
  • To elucidate the role of small GTPase heterodimerization in cellular growth responses.

Main Methods:

  • Utilized biochemical assays to study protein interactions.
  • Employed cell culture models to apply mechanical strain.
  • Investigated the function of specific small GTPases.

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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

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Main Results:

  • Demonstrated that cellular responses to mechanical strain are dependent on the heterodimerization of two specific small GTPases.
  • Identified the critical role of this heterodimerization in regulating cell growth under mechanical stress.
  • Provided molecular insights into how cells sense and respond to physical cues.

Conclusions:

  • The heterodimerization of specific small GTPases is essential for cellular adaptation to mechanical strain.
  • This finding offers a new molecular target for understanding and potentially modulating cellular mechanosensing.
  • Phuyal et al. (2022) highlight a novel mechanism in cell growth regulation.