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Related Experiment Video

Updated: Feb 1, 2026

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Does stromal interaction molecule-1 have five senses?

Peter B Stathopulos1, Mitsuhiko Ikura2

  • 1Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, London, ON, N6A 5C1, Canada.

Cell Calcium
|December 12, 2018
PubMed
Summary
This summary is machine-generated.

Stromal interaction molecule-1 (STIM1) uses its endoplasmic reticulum (ER) luminal domain for calcium (Ca2+) sensing. This finding challenges the long-held view that only the EF-hand loop controls STIM1

Keywords:
Calcium sensingEF-handEFSAMStromal interaction molecule-1

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Area of Science:

  • Molecular Cell Biology
  • Calcium Signaling
  • Ion Channel Regulation

Background:

  • Stromal interaction molecule-1 (STIM1) is a key regulator of store-operated calcium (SOC) entry.
  • Canonical EF-hand motifs in STIM1 were traditionally considered the primary calcium (Ca2+) sensors.
  • STIM1 activation leads to the opening of Orai1 calcium channels.

Purpose of the Study:

  • To investigate the role of the STIM1 endoplasmic reticulum (ER) luminal domain in calcium (Ca2+) sensing.
  • To challenge the established model of STIM1-mediated calcium channel activation.

Main Methods:

  • The study analyzed structural and functional data related to STIM1.
  • Investigated the STIM1 luminal domain's interaction with calcium ions (Ca2+).

Main Results:

  • Identified approximately five additional calcium (Ca2+) binding sites within the STIM1 ER luminal domain.
  • These sites contribute significantly to the sensing of extracellular calcium (Ca2+).

Conclusions:

  • The STIM1 ER luminal domain plays a crucial, previously unrecognized role in calcium (Ca2+) sensing.
  • This discovery proposes a new model for STIM1 activation and Orai1 channel regulation by calcium (Ca2+).