Related Experiment Video
Updated: Mar 21, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
The TRPCs, Orais and STIMs in ER/PM Junctions.
Dong Min Shin1, Aran Son2, Seonghee Park3
1Department of Oral Biology, BK 21 PLUS Project, Yonsei University College of Dentistry, Seoul, 120-752, South Korea. dmshin@yuhs.ac.
Calcium (Ca2+) signaling, crucial for cellular communication, is regulated at ER/PM junctions by STIM proteins interacting with Orai and TRPC channels. This interaction controls Ca2+ influx, impacting cellular responses.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Calcium (Ca2+) acts as a vital second messenger, initiating signals at endoplasmic reticulum/plasma membrane (ER/PM) junctions.
- This signaling pathway is sustained by Ca2+ influx through Orai and TRPC channels located at these ER/PM junctions.
Purpose of the Study:
- To explore the properties of TRPC and Orai channels and STIM proteins.
- To elucidate the mechanisms by which STIM interactions gate channel activity.
- To discuss the role of ER/PM junctions and their associated proteins in Ca2+ signaling.
Main Methods:
- Review of existing literature on STIM proteins, Orai channels, and TRPC channels.
- Analysis of protein interactions at ER/PM junctions.
- Discussion of Ca2+ influx mechanisms and regulation by STIMs and SARAF.
Main Results:
- STIM proteins form complexes with Orai and TRPC channels at ER/PM junctions, activating Ca2+ influx.
- STIM isoforms and SARAF modulate STIM1 function and Orai channel activity.
- ER/PM junctions are established by tethering proteins and can be PI(4,5)P2-poor or PI(4,5)P2-rich.
Conclusions:
- STIM-channel interactions are critical for regulating Ca2+ signaling.
- Understanding these interactions provides insights into cellular responses.
- Further research is needed to address open questions in the field of Ca2+ channel regulation.
More Related Videos
08:54Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
Published on: August 9, 2024
09:53Real-time In Vitro Monitoring of Odorant Receptor Activation by an Odorant in the Vapor Phase
Published on: April 23, 2019
Related Concept Videos
Directing Proteins to the Rough Endoplasmic Reticulum
Protein Translocation Machinery on 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...
Insertion of Multi-pass Transmembrane Proteins in the RER
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
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...
Insertion of Single-pass Transmembrane Proteins in the RER
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...
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...