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ER Retrieval Pathway

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

Protein Modifications in the RER

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...

The Endoplasmic Reticulum

The Endoplasmic Reticulum

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,...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

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...

Endoplasmic Reticulum

Endoplasmic Reticulum

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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Related Experiment Video

Updated: Aug 20, 2025

Investigation of Synaptic Tagging/Capture and Cross-capture using Acute Hippocampal Slices from Rodents

Investigation of Synaptic Tagging/Capture and Cross-capture using Acute Hippocampal Slices from Rodents

Published on: September 4, 2015

The endoplasmic reticulum puts a new spin on synaptic tagging.

Anja Konietzny¹, Susanne Wegmann², Marina Mikhaylova¹

¹AG Optobiology, Institute of Biology, Humboldt Universität zu Berlin, Berlin, Germany; Guest Group 'Neuronal Protein Transport', Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

Trends in Neurosciences

|November 25, 2022

Summary

Neurons utilize the endoplasmic reticulum (ER) to regulate synaptic plasticity. This review explores how ER is recruited to dendritic spines, influencing synaptic function and specificity.

Keywords:

calcium dendritic spine endoplasmic reticulum myosin phase separation spine apparatus synaptopodin

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Last Updated: Aug 20, 2025

Investigation of Synaptic Tagging/Capture and Cross-capture using Acute Hippocampal Slices from Rodents

Investigation of Synaptic Tagging/Capture and Cross-capture using Acute Hippocampal Slices from Rodents

Published on: September 4, 2015

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Published on: September 4, 2017

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Published on: May 7, 2013

Area of Science:

Neuroscience
Cell Biology
Synaptic Plasticity

Background:

The endoplasmic reticulum (ER) is a dynamic organelle crucial for cellular homeostasis, including protein/lipid synthesis and calcium regulation.
Neurons extensively utilize the ER to modulate synaptic properties and ensure specific synaptic input processing.

Purpose of the Study:

To review the mechanisms governing activity-dependent ER recruitment into dendritic spines.
To highlight the molecular players involved in ER transport and retention within spines.

Main Methods:

This review synthesizes existing literature on ER dynamics in neurons.
Focuses on molecular mechanisms, calcium signaling, and protein interactions.

Main Results:

Activity-dependent ER recruitment to dendritic spines fine-tunes synaptic properties.
Calcium signaling, synaptopodin 'tagging', and spine apparatus formation are key features.
Liquid-liquid phase separation is proposed as a potential driving force.

Conclusions:

ER dynamics within dendritic spines are critical for synaptic specificity and function.
Molecular mechanisms and biophysical processes like phase separation orchestrate ER localization and function in spines.