Evidence map›Paper›PMID 41792344›Full record

ArticleCellular and molecular life sciences : CMLS2026

A dual topology of STIM1 at the plasma membrane regulates calcium constitutive entry.

Paul Buscaglia, Nelig Le Goux, Patrice Hemon, Anthony Mainguy, Maela Hus, Mathieu Gimaray, Paul Roger Claude Imbert, Alix A J Rouault, Julien A Sebag, Olivier Mignen

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Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Paul BuscagliaLBAI, UMR1227, University Brest, Inserm, Brest, France.
Nelig Le GouxLBAI, UMR1227, University Brest, Inserm, Brest, France. nelig.legoux@qmul.ac.uk.ORCID http://orcid.org/0009-0002-5904-3606
Patrice HemonLBAI, UMR1227, University Brest, Inserm, Brest, France.
Anthony MainguyLBAI, UMR1227, University Brest, Inserm, Brest, France.
Maela HusLBAI, UMR1227, University Brest, Inserm, Brest, France.
Mathieu GimarayLBAI, UMR1227, University Brest, Inserm, Brest, France.
Paul Roger Claude ImbertCentre for Microvascular Research, William Harvey Research Institute, Queen Mary University of London, London, EC1M 6BQ, UK.
Alix A J RouaultDepartment of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, 52242, USA.
Julien A SebagDepartment of Pharmacology, University of Michigan, Ann Arbor, MI, 48109, USA.
Olivier MignenLBAI, UMR1227, University Brest, Inserm, Brest, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

STIM1, a type I transmembrane protein characterized by its extracellular N-terminal domain (STIM1PM), was initially identified as a plasma membrane (PM)-localized protein with tumor growth suppressor activity. Subsequent studies have identified a role for STIM1PM in the regulation of store-independent Ca2+ entry pathways including arachidonic acid-regulated Ca2+ (ARC) channels and constitutive Ca2+ entry (CCE). Mechanistically, N-glycosylation facilitates STIM1PM trafficking and stability at the PM. In this study, we demonstrate that STIM1PM uniquely exhibits dual topology at the PM, presenting both the expected type I orientation and an alternative type II orientation. Notably, we found that both orientations of STIM1PM contribute to CCE regulation. Our results confirm that N-glycosylation promotes the N-terminal-out orientation of STIM1PM, however, here we found it also modulates it’s the receptor’s dual topology. Our findings reveal that STIM1PM displays dual topology and regulate CCE.

Indexed as

CalciumCell MembraneNeoplasm ProteinsStromal Interaction Molecule 1Calcium ChannelsCalcium SignalingGlycosylationHEK293 CellsHumansProtein DomainsProtein TransportCalciumCalcium ChannelsNeoplasm ProteinsSTIM1 protein, humanStromal Interaction Molecule 1Antiparallel dimersConstitutive Ca2+ entryDual topologyPlasma membraneRegulationSTIM1PM

Identifiers

PMID41792344
PMCPMC13003068

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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.