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

Cotranslational Protein Translocation01:20

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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Protein Translocation Machinery on the ER Membrane01:28

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.
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

You might also read

Related Articles

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

Sort by
Same author

Regulation of Orai1/STIM1 mediated I<sub>CRAC</sub> by intracellular pH.

Scientific reports·2017
Same author

Curcumin inhibits activation of TRPM2 channels in rat hepatocytes.

Redox biology·2015
Same author

The predominant role of IP₃ type 1 receptors in activation of store-operated Ca²+ entry in liver cells.

Biochimica et biophysica acta·2010
Same author

Increasing cycles of intermittent ischemia can effectively maintain liver function during the acute phase of ischemia reperfusion injury by promotion of bile flow and reduction in bile salt toxicity.

Digestive surgery·2010
Same author

Properties of Orai1 mediated store-operated current depend on the expression levels of STIM1 and Orai1 proteins.

The Journal of physiology·2009
Same author

Insulin potentiates EGFR activation and signaling in fibroblasts.

Biochemical and biophysical research communications·2004

Related Experiment Video

Updated: Jul 11, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

TRPC1 Ca(2+)-permeable channels in animal cells.

G Rychkov1, G J Barritt

  • 1School of Molecular and Biomedical Science, University of Adelaide, 5005 Adelaide, South Australia, Australia.

Handbook of Experimental Pharmacology
|January 16, 2007
PubMed
Summary

Transient Receptor Potential Canonical 1 (TRPC1) is a key ion channel protein involved in various cellular functions, including neuronal growth cone turning. Further research is needed to fully understand TRPC1

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Ion Channel Physiology

Background:

  • Transient Receptor Potential Canonical 1 (TRPC1) is an integral membrane protein with six transmembrane domains.
  • TRPC1 has N-terminal ankyrin repeat motifs and interacts with various cellular proteins like calmodulin and InsP3 receptor.
  • Studies on TRPC1 function are challenging due to difficulties in obtaining high-affinity, specific antibodies.

Purpose of the Study:

  • To investigate the structure, function, and cellular roles of the TRPC1 protein.
  • To explore the mechanisms of TRPC1 activation and its involvement in cation channels.
  • To highlight the challenges and future directions in TRPC1 research.

Main Methods:

  • Analysis of TRPC1 polypeptide structure and topology.

More Related Videos

Controllable Ion Channel Expression through Inducible Transient Transfection
10:00

Controllable Ion Channel Expression through Inducible Transient Transfection

Published on: February 17, 2017

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Related Experiment Videos

Last Updated: Jul 11, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

Controllable Ion Channel Expression through Inducible Transient Transfection
10:00

Controllable Ion Channel Expression through Inducible Transient Transfection

Published on: February 17, 2017

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

  • Utilizing antibodies to study endogenous TRPC1 and employing ectopic expression systems.
  • Investigating TRPC1 interactions with other proteins and its role in cation channel formation.

    • Main Results:

    • TRPC1 forms heterotetramers with other TRPC proteins, contributing to non-selective cation channels.
    • TRPC1 is implicated in store-operated Ca2+ channels (SOCs) and activated by stretch or InsP3R.
    • Activation of TRPC1 facilitates Na+ and Ca2+ entry, with Ca2+ providing feedback inhibition.

    Conclusions:

    • TRPC1 plays a critical role in numerous downstream cellular pathways, notably in neuronal growth cone turning.
    • The exact mechanisms of TRPC1 activation and its diverse functions require further experimental resolution.
    • TRPC1 presents a fascinating area of study due to its wide-ranging roles and the complexities in elucidating its precise functions.