Results 61 to 70 of about 7,759 (184)
Glia, Volume 74, Issue 9, September 2026.Astrocytic TREK‐1‐dependent volume transients contribute to hippocampal synaptic plasticity and memory formation. TRPA1‐mediated astrocytic calcium signaling is required for long‐term potentiation, while astrocytic BDNF is necessary and sufficient to support sustained synaptic plasticity.
Victor James Drew +6 more
wiley +1 more source
A cholesterol interaction domain in STIM1 is important for STIM1‐Orai1 coupling (LB53)
The FASEB Journal, 2014 STIM1 and Orai1 are the basic components of the calcium influx pathway known as store‐operated calcium entry (SOCE). STIM1 is a calcium sensor, which oligomerizes and activates Orai channels when calcium levels drop inside the endoplasmic reticulum. The activation of Orai1 requires the direct coupling of STIM1 domain known as SOAR (Stim Orai Activating
Jonathan Pacheco, Luis Vaca
openaire +1 more source
TRPC channels as STIM1-regulated SOCs [PDF]
Channels, 2009 Store-operated Ca(2+) channels (SOCs) are Ca(2+) influx channels at the plasma membrane whose opening is determined by the level of Ca(2+) stored in the endoplasmic reticulum lumen. SOCs are activated in response to receptor-mediated or passive depletion of ER Ca(2+) to regulate many Ca(2+)-dependent cellular functions.
Joseph P, Yuan +6 more
openaire +2 more sources
Mapping the Proximity Interaction Network of STIM1 Reveals New Mechanisms of Cytoskeletal Regulation
Cells, 2021 Stromal interaction molecule 1 (STIM1) resides primarily in the sarco/endoplasmic reticulum, where it senses intraluminal Ca2+ levels and activates Orai channels on the plasma membrane to initiate Ca2+ influx.
Jesse Gammons +2 more
doaj +1 more source
Evolutionarily conserved hydrophobicity and sterics in TM3/TM4 balance Orai1 pore opening
Protein Science, Volume 35, Issue 8, August 2026.Abstract The calcium (Ca2+) channel Orai1—the pore‐forming subunit of the Ca2+ release‐activated Ca2+ channel—is opened by its physiological activator, the endoplasmic reticulum (ER)‐resident Ca2+ sensor stromal interaction molecule 1 (STIM1) upon ER Ca2+ store‐depletion.
Maximilian Fröhlich +17 more
wiley +1 more source
The SOAR of STIM1 interacts with plasma membrane lipids to form ER-PM contact sites
Cell Reports, 2023 Summary: Depletion of Ca2+ from the endoplasmic reticulum (ER) causes the ER Ca2+ sensor STIM1 to form membrane contact sites (MCSs) with the plasma membrane (PM). At the ER-PM MCS, STIM1 binds to Orai channels to induce cellular Ca2+ entry.
Hadas Achildiev Cohen +4 more
doaj +1 more source
British Journal of Pharmacology, Volume 183, Issue 15, Page 4091-4110, August 2026.Abstract Catecholamines are classically viewed as neuronal transmitters and adrenal hormones; however, accumulating evidence demonstrates that sources other than nerve fibres and adrenal medulla play a fundamental role in local organ regulation. Physiological paradoxes, such as preserved organ function after denervation or transplantation, challenge a ...
Mariana G. de Oliveira +3 more
wiley +1 more source
Understanding the STIM1-ulous [PDF]
Science, 2013 Signal Transduction![Figure][1] CREDIT: ALEJANDRO P. ADAM, PETER A. VINCENT, AND MOHAMED TREBAK The permeability of the circulatory system is carefully regulated, and disruption of the barrier can contribute to inflammation and sepsis. One important means of regulation is the action of thrombin on vascular endothelial cells.
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Alzheimer's &Dementia, Volume 22, Issue 7, July 2026.Abstract INTRODUCTION Chronic neuroinflammation in Alzheimer's disease (AD) alters astrocyte physiology and neurovascular unit function. AD patients frequently experience recurrent systemic inflammatory insults from comorbid conditions, which act as “secondary‐hits” believed to worsen cognitive decline.
Chang Liu +4 more
wiley +1 more source
STIM1 long and STIM1 gate differently TRPC1 during store-operated calcium entry
Cell Calcium, 2020 During myogenesis, a long splice variant of STIM1, called STIM1L is getting expressed, while the level of STIM1 remains constant. Previous work demonstrated that STIM1L is more efficient in eliciting store-operated Ca2+ entry (SOCE), but no current analysis of the channel(s) activated by this new STIM1L isoform was performed until now.
Dyrda, Agnieszka +2 more
openaire +4 more sources