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Article

Phosphorylation of STIM1 at ERK1/2 target sites regulates interaction with the microtubule plus-end binding protein EB1.

Journal of cell science - 15 Jul 2013

Pozo-Guisado Eulalia, Casas-Rua Vanessa, Tomas-Martin Patricia, Lopez-Guerrero Aida M, Alvarez-Barrientos Alberto, Martin-Romero Francisco Javier

Abstract excerpt

STIM1 (stromal interaction molecule 1) is a key regulator of store-operated calcium entry (SOCE). Upon depletion of Ca(2+) concentration within the endoplasmic reticulum (ER), STIM1 relocalizes at ER-plasma membrane junctions, activating store-operated calcium channels (SOCs). Although the molecular details for STIM1-SOC binding is known, the regulation of SOCE remains largely unknown. A detailed list of...

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Source

Identifiers

PMID: 23687376
DOI: 10.1242/jcs.125054

Genes

STIM1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Phosphorylation of STIM1 at ERK1/2 target sites regulates interaction with the microtubule plus-end binding protein EB1.PMID 23687376Read ↗

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