Proteomics

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The ER stress sensor IRE1 interacts with STIM1 to promote store-operated calcium entry, T cell activation, and muscular differentiation

ABSTRACT: A quantitative phosphoproteomic study was performed on mouse embryonic fibroblasts (MEF) knocked-out of IRE1 protein and re rexpressin it culturen in 25mM glucose media. The chosen experimental strategy was to perform phosphopeptide enrichment associated with multiplex protein identification and quantification by LC-MSMS on a high-resolution mass spectrometer using tandem mass tag (TMT9; Thermo Fisher Scientific) technology and High- Select Fe-NTA Phosphopeptide Enrichment Kit (Thermo Fisher Scientific).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Embryonic Fibroblast, Fibroblast

SUBMITTER: Amado Carreras  

LAB HEAD: Amado Carreras Sureda

PROVIDER: PXD046579 | Pride | 2023-12-08

REPOSITORIES: Pride

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The ER stress sensor IRE1 interacts with STIM1 to promote store-operated calcium entry, T cell activation, and muscular differentiation.

Carreras-Sureda Amado A   Zhang Xin X   Laubry Loann L   Brunetti Jessica J   Koenig Stéphane S   Wang Xiaoxia X   Castelbou Cyril C   Hetz Claudio C   Liu Yong Y   Frieden Maud M   Demaurex Nicolas N  

Cell reports 20231205 12

Store-operated Ca<sup>2+</sup> entry (SOCE) mediated by stromal interacting molecule (STIM)-gated ORAI channels at endoplasmic reticulum (ER) and plasma membrane (PM) contact sites maintains adequate levels of Ca<sup>2+</sup> within the ER lumen during Ca<sup>2+</sup> signaling. Disruption of ER Ca<sup>2+</sup> homeostasis activates the unfolded protein response (UPR) to restore proteostasis. Here, we report that the UPR transducer inositol-requiring enzyme 1 (IRE1) interacts with STIM1, promote  ...[more]

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