Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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,...

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,...

Endoplasmic Reticulum

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer membrane of the nucleus. This structural continuity integrates nuclear and cytoplasmic processes and facilitates efficient intracellular transport. This allows mRNA to move directly from the nucleus to ribosomes for efficient protein synthesis. As a result, the ER serves as a central site for the synthesis, processing, and distribution of...

Golgi Apparatus

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...

Golgi Apparatus

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...

Golgi Apparatus

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...

You might also read

Related Articles

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

Sort by

Same author

Autophagy inhibition induces AML cell death and enhances the efficacy of chemotherapy under hypoxia.

bioRxiv : the preprint server for biology·2024

Same author

Human atlastin-3 is a constitutive ER membrane fusion catalyst.

The Journal of cell biology·2023

Same author

Membrane fusion by <i>Drosophila</i> atlastin does not require GTP hydrolysis.

Molecular biology of the cell·2022

Same author

Reconstitution of human atlastin fusion activity reveals autoinhibition by the C terminus.

The Journal of cell biology·2021

Same author

Inhibiting autophagy targets human leukemic stem cells and hypoxic AML blasts by disrupting mitochondrial homeostasis.

Blood advances·2021

Same author

GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion.

The Journal of cell biology·2018

Same journal

Mechanisms underpinning chromosome structure in metazoans.

Molecular biology of the cell·2026

Same journal

Conserved and Divergent Modes of Substrate Interaction Define Selective Localizations and Functions of a Cdc14 Phosphatase.

Molecular biology of the cell·2026

Same journal

Dimerization of the centriolin-like protein Nud1 governs spindle pole body inheritance in budding yeast.

Molecular biology of the cell·2026

Same journal

Non-muscle Myosin II acts as a negative feedback mediator to control cell contraction dynamics in adherent cells.

Molecular biology of the cell·2026

Same journal

The tetraspanin disc proteins, peripherin-2 and ROM1, facilitate CNG channel localization to the rod outer segment.

Molecular biology of the cell·2026

Same journal

Csf1 facilitates adaptive membrane lipid remodeling linked to ER-plasma membrane contact sites.

Molecular biology of the cell·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 15, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

Yip1A structures the mammalian endoplasmic reticulum.

Kaitlyn M Dykstra¹, Jacqueline E Pokusa, Joseph Suhan

¹Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

Molecular Biology of the Cell

|March 19, 2010

Summary

This summary is machine-generated.

Yip1A protein is crucial for maintaining endoplasmic reticulum (ER) network structure and efficient cargo export. Its depletion causes ER whorl formation and slows protein transport.

More Related Videos

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

Drosophila Embryo Preparation and Microinjection for Live Cell Microscopy Performed using an Automated High Content Analyzer

Drosophila Embryo Preparation and Microinjection for Live Cell Microscopy Performed using an Automated High Content Analyzer

Published on: January 19, 2021

Related Experiment Videos

Last Updated: Jun 15, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

Drosophila Embryo Preparation and Microinjection for Live Cell Microscopy Performed using an Automated High Content Analyzer

Drosophila Embryo Preparation and Microinjection for Live Cell Microscopy Performed using an Automated High Content Analyzer

Published on: January 19, 2021

Area of Science:

Cell Biology
Molecular Biology
Membrane Trafficking

Background:

The endoplasmic reticulum (ER) undergoes dynamic structural changes in specialized cells.
ER reorganization into concentric whorls is observed, but mechanisms and cargo export roles are unclear.

Purpose of the Study:

To identify key mediators of ER organization and their role in cargo export.
To elucidate the function of Yip1A in ER structure and protein transport.

Main Methods:

Depletion of Yip1A protein in cells.
Analysis of ER morphology using microscopy.
Assessing coat protein (COP)II-mediated protein export rates.
Site-directed mutagenesis of Yip1A.

Main Results:

Yip1A depletion caused ER restructuring into concentric whorls.
Whorl formation significantly slowed COPII-mediated protein export.
Altering a single amino acid in Yip1A abolished its ER network dispersal function.

Conclusions:

Yip1A is a conserved mediator of ER organization and regulates ER network dispersal.
Yip1A plays a critical role in facilitating efficient cargo export from the ER.
ER membrane organization by Yip1A is essential for timely protein transport.