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

Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Cell-surface Signaling01:21

Cell-surface Signaling

Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.
Signal Transduction: Overview01:26

Signal Transduction: Overview

Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...

You might also read

Related Articles

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

Sort by
Same author

Lipid Analysis in Live <i>Caenorhabditis elegans</i> Using Solution-State NMR Spectroscopy.

Bio-protocol·2026
Same author

Unsaturated fatty acids are required for germline proliferation and membrane structural integrity in Caenorhabditis elegans.

Genetics·2025
Same author

Unsaturated Fatty Acids Are Required for Germline Proliferation and Membrane Structural Integrity in <i>Caenorhabditis elegans</i>.

bioRxiv : the preprint server for biology·2025
Same author

Fatty acid synthesis and utilization in gram-positive bacteria: insights from <i>Bacillus subtilis</i>.

Microbiology and molecular biology reviews : MMBR·2025
Same author

Membranes, where lipids and protein meet.

Chemistry and physics of lipids·2025
Same author

An inducible and reversible system to regulate unsaturated fatty acid biosynthesis in C. elegans.

G3 (Bethesda, Md.)·2025

Related Experiment Video

Updated: Jun 2, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Playing with transmembrane signals.

Larisa E Cybulski1, Diego de Mendoza

  • 1Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET) and Departamento de Microbiología; Facultad de Ciencias Bioquímicas y Farmacéuticas; Universidad Nacional de Rosario; Rosario, Santa Fe Argentina.

Communicative & Integrative Biology
|April 22, 2011
PubMed
Summary
This summary is machine-generated.

Researchers created a minimal bacterial cold sensor by simplifying the DesK protein. This breakthrough reveals how transmembrane segments transmit signals, offering a new method to study membrane protein function.

Keywords:
lipidsmembranesnanosensorsignal transductiontranscriptional regulationtransmembrane signaling

More Related Videos

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
12:24

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Published on: September 29, 2016

Optogenetic Signaling Activation in Zebrafish Embryos
07:18

Optogenetic Signaling Activation in Zebrafish Embryos

Published on: October 27, 2023

Related Experiment Videos

Last Updated: Jun 2, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
12:24

Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

Published on: September 29, 2016

Optogenetic Signaling Activation in Zebrafish Embryos
07:18

Optogenetic Signaling Activation in Zebrafish Embryos

Published on: October 27, 2023

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Membrane proteins are vital for cellular processes, often featuring transmembrane (TM) segments.
  • Understanding how TM segments change to enable signaling is crucial but poorly understood.
  • DesK, a bacterial cold sensor with five TM segments, exemplifies this signaling complexity.

Purpose of the Study:

  • To investigate the molecular mechanisms of signal sensing and transmission in membrane proteins.
  • To develop a simplified system for studying complex membrane protein functions.
  • To uncover the signaling pathway of the bacterial cold sensor DesK.

Main Methods:

  • Constructing a chimeric, single membrane-spanning minimal sensor based on DesK.
  • Employing a reductionist approach to isolate key functional components.
  • Analyzing the sensing and signal transmission capabilities of the minimal sensor.

Main Results:

  • Successfully captured both sensing and transmission functions in a minimal DesK sensor.
  • Demonstrated that a single TM segment can suffice for cold sensing and signal relay.
  • Validated the 'minimalist' approach for studying complex biological systems.

Conclusions:

  • The study provides insights into the fundamental principles of membrane protein signaling.
  • The developed minimal sensor serves as a powerful tool for future research.
  • This work introduces a novel strategy for dissecting TM domain-mediated signal transduction.