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

Formation of Lipopolysaccharides

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...

Bacterial Translocation and Protein Secretion

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...

Phosphoinositides and PIPs

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

Cytoskeletal Linker Proteins - Plakins

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...

You might also read

Related Articles

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

Sort by

Same author

VPS13C/PARK23 initiates lipid transfer and membrane remodeling for efficient lysosomal repair.

Nature communications·2026

Same author

Steric repulsion counteracts ER-to-lipid droplet protein movement.

Science advances·2025

Same author

RpH-ILV: Probe for lysosomal pH and acute LLOMe-induced membrane permeabilization in cell lines and <i>Drosophila</i>.

Science advances·2025

Same author

Structure of the yeast ceramide synthase.

Nature structural & molecular biology·2024

Same author

Author Correction: Structure of the endosomal CORVET tethering complex.

Nature communications·2024

Same author

Structure of the endosomal CORVET tethering complex.

Nature communications·2024

Search research articles

Related Experiment Video

Updated: Apr 25, 2026

Imaging Plasma Membrane Deformations With pTIRFM

Imaging Plasma Membrane Deformations With pTIRFM

Published on: April 2, 2014

Building bridges: BLTP2 forms ER-plasma membrane contact sites.

Florian Fröhlich^1,2

¹Department of Biology/Chemistry, Bioanalytical Chemistry Section, Osnabrück University, Osnabrück, Germany.

The Journal of Cell Biology

|April 24, 2026

Summary

This summary is machine-generated.

Bridge-like lipid-transport protein 2 (BLTP2) facilitates lipid transfer at membrane contact sites. This study identifies a conserved endoplasmic reticulum-plasma membrane contact site mediated by BLTP2.

More Related Videos

Real-time Imaging of Leukotriene B4 Mediated Cell Migration and BLT1 Interactions with β-arrestin

Real-time Imaging of Leukotriene B4 Mediated Cell Migration and BLT1 Interactions with β-arrestin

Published on: December 23, 2010

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Related Experiment Videos

Last Updated: Apr 25, 2026

Imaging Plasma Membrane Deformations With pTIRFM

Imaging Plasma Membrane Deformations With pTIRFM

Published on: April 2, 2014

Real-time Imaging of Leukotriene B4 Mediated Cell Migration and BLT1 Interactions with β-arrestin

Real-time Imaging of Leukotriene B4 Mediated Cell Migration and BLT1 Interactions with β-arrestin

Published on: December 23, 2010

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Area of Science:

Cell biology
Membrane biology
Lipid transport

Background:

Bridge-like lipid-transport protein 2 (BLTP2) is involved in lipid transfer.
The precise localization and function of BLTP2 at membrane contact sites remain unclear.

Purpose of the Study:

To identify and characterize the specific membrane contact sites mediated by BLTP2.
To elucidate the role of BLTP2 in connecting the endoplasmic reticulum and plasma membrane.

Main Methods:

Immunofluorescence microscopy
Biochemical assays
Genetic manipulation

Main Results:

BLTP2 mediates a conserved contact site between the endoplasmic reticulum and the plasma membrane.
Characterization of the BLTP2-dependent contact site reveals its role in lipid transport.
Identification of key domains within BLTP2 responsible for membrane tethering.

Conclusions:

BLTP2 is a crucial protein for establishing and maintaining endoplasmic reticulum-plasma membrane contact sites.
These BLTP2-mediated contact sites are important for cellular lipid homeostasis.
Further research into BLTP2 function could reveal new therapeutic targets for lipid-related disorders.