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STIM1 is cleaved by calpain
Author(s) -
Prins Daniel,
Michalak Marek
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.09.015
Subject(s) - calpain , stim1 , orai1 , microbiology and biotechnology , proteases , calpastatin , chemistry , cytoplasm , cleavage (geology) , endoplasmic reticulum , apoptosis , biophysics , biology , biochemistry , enzyme , paleontology , fracture (geology)
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.