Evidence map›Paper›PMID 41233214›Full record

ArticleTrends in cell biology2025

A STIMulating new view of activity-dependent membrane contact architecture.

Eamonn J Dickson

Abstract readComment
In one paragraph

Article in Trends in cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Eamonn J DicksonDepartment of Physiology and Membrane Biology, University of California, Davis, CA 95616, USA. Electronic address: ejdickson@health.ucdavis.edu.

Funding

Alpha-Synuclein aberrantly modifies the nanoscale distribution and function of ion channels to promote neuronal cytotoxicityRF1NS131379 · NINDS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI DICKSON, EAMONN JAMES · 2023 to 2023
$1.7M
Lysosomal control of plasma membrane -endoplasmic reticulum membrane contacts regulates neuronal excitabilityR35GM149211 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Eamonn James Dickson · 2023 to 2026
$1.5M
NIGMS NIH HHS R35 GM149211NINDS NIH HHS RF1 NS131379
6 · The paper itself

Abstract

Chhikara et al. reframe stromal interaction molecule (STIM) proteins as structural organizers of membrane contact sites, not just calcium-entry activators, in neurons. STIM2 maintains resting endoplasmic reticulum (ER)-plasma membrane (PM) junctions; STIM1 dynamically expands them during neuronal activity. This activity-dependent remodeling tunes ER-PM proximity and calcium coupling, shifting focus from channel gating to spatial organization.

Indexed as

Cell MembraneAnimalsCalciumEndoplasmic ReticulumHumansMembrane ProteinsNeuronsStromal Interaction Molecule 1Stromal Interaction MoleculesCalciumMembrane ProteinsStromal Interaction Molecule 1Stromal Interaction Moleculescalciumdendritic microdomainsER–PM junctionsNMDAR-dependent remodelingSTIM1/STIM2store-operated Ca(2+) entry (SOCE)

Identifiers

PMID41233214
PMCPMC13250728

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.