Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Endoplasmic Reticulum01:39

Endoplasmic Reticulum

106.9K
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.
106.9K
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

21.1K
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,...
21.1K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

17.2K
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...
17.2K
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

7.8K
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...
7.8K
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

80.8K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
80.8K
Enlargement of the Plasma Membrane01:22

Enlargement of the Plasma Membrane

2.3K
Cell division and enlargement are processes that require precise control. The control ensures that cell division cannot proceed unless the cell has grown to a specific size. A spherical, dividing cell requires an approximately 1.6X increase in its surface area to double its volume. The secretory pathway also has a significant role in cell membrane enlargement. Secretory vesicles that bud off from the Golgi apparatus and later fuse with the plasma membrane during exocytosis are a major source of...
2.3K

You might also read

Related Articles

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

Sort by
Same author

A programmable benchtop photocrosslinking chamber for controlled bioconjugation.

HardwareX·2026
Same author

SIRT3/AARS2 regulates SOD2 lactylation to determine neuronal fate in TBI.

Molecular neurobiology·2026
Same author

<i>In situ</i> SERS reveals nickel hydroxide formation in PtRuNi catalysts enhances hydrogen oxidation.

Nanoscale advances·2026
Same author

LncRNA TUG1 promotes hypertrophic scar formation via the miR-627/IGF1R axis.

Journal of molecular histology·2026
Same author

Exploring the relationship between oxidative balance score and sex hormone levels in American males: a cross-sectional study.

Hormones (Athens, Greece)·2026
Same author

Synergy of Mott-Schottky heterojunction and sulfur vacancies toward high-efficiency water splitting.

Journal of colloid and interface science·2026

Related Experiment Video

Updated: Jan 23, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
16:43

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

13.6K

Manipulating Endoplasmic Reticulum-Plasma Membrane Tethering in Plants Through Fluorescent Protein Complementation.

Kai Tao1,2, Justin R Waletich2, Felipe Arredondo2

  • 1Molecular and Cellular Biology Program, Oregon State University, Corvallis, OR, United States.

Frontiers in Plant Science
|June 14, 2019
PubMed
Summary

The bimolecular fluorescence complementation (BiFC) assay can unintentionally create artificial endoplasmic reticulum (ER)-plasma membrane (PM) tethers in plants. This artifact, caused by protein interactions, may lead to misinterpreting protein localization and interactions in published studies.

Keywords:
endoplasmic recticulumintegral membrane proteinperipheral membrane proteinplasma membranetethering

More Related Videos

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.7K
Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

14.7K

Related Experiment Videos

Last Updated: Jan 23, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
16:43

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

13.6K
Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.7K
Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

14.7K

Area of Science:

  • Plant Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • The bimolecular fluorescence complementation (BiFC) assay is commonly used to study protein-protein interactions at the plasma membrane (PM).
  • Investigating receptor-like kinases (RLKs) and remorins in *Nicotiana benthamiana* revealed unexpected fluorescence patterns.
  • These patterns resembled those caused by the endoplasmic reticulum (ER)-PM tether protein Synaptotagmin1 (SYT1).

Purpose of the Study:

  • To investigate the cause of heterogeneous fluorescence distribution observed during BiFC assays in plant cells.
  • To determine if BiFC can lead to artifactual ER-PM tethering.
  • To assess the implications of these findings for the interpretation of BiFC studies in plants.

Main Methods:

  • Utilized bimolecular fluorescence complementation (BiFC) assays in *Nicotiana benthamiana* leaf cortical cells.
  • Performed domain swap experiments with Synaptotagmin1 (SYT1).
  • Tested interactions between integral membrane proteins and PM-targeted peripheral membrane proteins using BiFC.

Main Results:

  • Observed unexpected fluorescence patterns co-localizing with ER and ER-PM contact sites.
  • Inferred that non-specific dimerization in BiFC can create artificial ER-PM tethers analogous to SYT1.
  • Demonstrated that BiFC complexes can trap integral membrane proteins in the ER, forming PM-ER tethers.

Conclusions:

  • Spontaneous BiFC complex maturation can lead to artifactual ER-PM tethering, potentially altering cellular structures.
  • The BiFC assay may risk misinterpreting protein-protein interactions and membrane organization in plants.
  • Published BiFC studies on plant membrane proteins may require re-evaluation due to potential artifacts.