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A dual topology of STIM1 at the plasma membrane regulates calcium constitutive entry
Journal article   Open access   Peer reviewed

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 and Olivier Mignen
Cellular and molecular life sciences : CMLS, Vol.83(1), 161
12/2026
DOI: 10.1007/s00018-026-06141-0
PMCID: PMC13003068
PMID: 41792344
url
https://doi.org/10.1007/s00018-026-06141-0View
Published (Version of record) Open Access

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.
 Regulation Dual topology STIM1PM Antiparallel dimers Plasma membrane Constitutive Ca2+ entry

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