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

Thermosensation

Thermosensation

Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...

Insertion of Multi-pass Transmembrane Proteins in the RER

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...

Cotranslational Protein Translocation

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

Repressible Operon: trp Operon

Repressible Operon: trp Operon

The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...

Protein Translocation Machinery on the ER Membrane

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

Protein Transport to the Thylakoids

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...

You might also read

Related Articles

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

Sort by

Same author

Pancreatitis: correcting CFTR expression and function as a promising effective treatment.

Frontiers in physiology·2026

Same author

Transient changes in body weight and behavior during the placentation period in non-human primates and rodents.

Scientific reports·2026

Same author

Role of Innate Oral Immunity and the Salivary Fluid in Inflammatory Bowel Disease.

Cellular and molecular gastroenterology and hepatology·2025

Same author

Human chorionic gonadotropin inhibits locomotion but not food intake independently of the area postrema and the nucleus tractus solitarius in female mice.

Physiology & behavior·2025

Same author

Functional expression of the proton channel OTOP1 in brown adipocytes.

Biochemical and biophysical research communications·2025

Same author

Transmembrane channel-like 4 (TMC4) could act as a negative regulator of KCNQ1 (Kv7.1) potassium channel.

Biochimica et biophysica acta. Biomembranes·2025

Search research articles

Related Experiment Video

Updated: Jun 14, 2026

Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

Published on: January 21, 2022

Opening the TRPML gates.

Soichiro Yamaguchi¹, Shmuel Muallem

¹Department of Physiology, University of Texas, Southwestern Medical center, Dallas, TX 75390, USA.

Chemistry & Biology

|March 27, 2010

Summary

This summary is machine-generated.

Researchers discovered new ways to activate TRPML3 channels using a high-throughput chemical screen. This breakthrough will help scientists fully understand the biological roles of these important cellular channels.

More Related Videos

Purification of Endogenous Drosophila Transient Receptor Potential Channels

Purification of Endogenous Drosophila Transient Receptor Potential Channels

Published on: December 28, 2021

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

Related Experiment Videos

Last Updated: Jun 14, 2026

Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

Published on: January 21, 2022

Purification of Endogenous Drosophila Transient Receptor Potential Channels

Purification of Endogenous Drosophila Transient Receptor Potential Channels

Published on: December 28, 2021

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

Area of Science:

Molecular Biology
Cellular Biology
Pharmacology

Background:

The intracellular TRPML (transient receptor potential mucolipin) channels are crucial for various biological processes.
However, the specific physiological stimuli that activate these channels have remained largely unknown.
Understanding TRPML channel activation is key to elucidating their functions.

Discussion:

Grimm et al. conducted a high-throughput chemical screen to identify compounds that activate TRPML channels.
The screen successfully identified numerous selective activators for TRPML3.
These findings provide valuable tools for further investigation.

Key Insights:

A large-scale chemical screen has identified novel selective activators of TRPML3 channels.
This discovery addresses a significant gap in understanding TRPML channel physiology.
The identified compounds are expected to facilitate detailed characterization of TRPML3.

Outlook:

The newly identified TRPML3 activators will enable comprehensive studies of TRPML3 channel function.
Further research can now focus on the precise physiological roles of TRPML3.
This work paves the way for potential therapeutic strategies targeting TRPML channels.