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Related Experiment Video

Updated: Apr 1, 2026

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

Published on: July 21, 2021

STIM1 is cleaved by calpain.

Daniel Prins¹, Marek Michalak¹

¹Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2S7, Canada.

|October 11, 2015

Summary

Calpain proteases cleave STIM1, a key protein in store-operated calcium entry (SOCE). This cleavage regulates STIM1 levels, particularly during cellular stress and apoptosis, offering insights into disease mechanisms.

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Store-operated calcium entry (SOCE) regulates intracellular calcium levels.
SOCE is primarily mediated by STIM1 and Orai1 proteins.
STIM1 dysregulation is linked to various human diseases.

Purpose of the Study:

To investigate the regulation of STIM1 protein abundance.
To identify potential mechanisms controlling STIM1 levels in cellular stress.
To explore the role of proteases in STIM1 regulation.

Main Methods:

Biochemical assays to identify STIM1 cleavage sites.
Protease activity assays using calpains.
Western blotting to assess STIM1 levels under stress conditions.

Keywords:

Calpain Store-operated calcium entry Stromal interaction molecule 1

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Apoptosis induction and analysis of STIM1 cleavage.

Main Results:

The cytoplasmic domain of STIM1 is identified as a substrate for calpains.
Calpain-mediated cleavage of STIM1 controls its cellular abundance.
STIM1 cleavage by calpains is significantly increased during cellular stress and apoptosis.

Conclusions:

Calpain proteases regulate STIM1 protein levels through direct cleavage.
This mechanism provides a novel way to control STIM1 abundance, especially under stress.
Understanding STIM1 regulation by calpains may offer therapeutic targets for diseases associated with STIM1 dysregulation.