STIM1 is cleaved by calpain. Issue 21 (8th October 2015)

• Record Type: Journal Article
• Authors: Prins, Daniel; Michalak, Marek
• Is Part Of: FEBS letters. Volume 589:Issue 21(2015)
• Page Start: 3294
• Page End: 3301
• Publication Date: 2015-10-08
• Subjects: Calpain -- Store-operated calcium entry -- Stromal interaction molecule 1; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.09.015
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Store‐operated calcium entry (SOCE) is a pathway that moves Ca 2+ across the plasma membrane and is mediated by two major proteins, STIM1 and Orai1. Here, we discovered that the cytoplasmic domain of STIM1 is a target for calpains, a family of Ca 2+ ‐activated proteases. We found that calpain cleavage of STIM1 serves to control its cellular abundance and was noticeably increased under conditions of cellular stress and apoptosis. Dysregulation of STIM1 levels has been reported to have human disease consequences and our results suggest a mechanism for controlling STIM1 abundance. Abstract : The cytoplasmic domain of STIM1 is cleaved by calpains. Inhibition of calpain activity increases STIM1 abundance. Calpain cleavage of STIM1 is enhanced in apoptotic cells. STIM1 cleavage requires Ca 2+ entry via Orai1.