Calmodulin dissociates the STIM1-Orai1 complex and STIM1 oligomers.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29051492.
- Also identified by DOI 10.1038/s41467-017-01135-w and PMC identifier 5648805.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Store-operated calcium entry (SOCE) is a major pathway for calcium ions influx into cells and has a critical role in various cell functions. Here we demonstrate that calcium-bound calmodulin (Ca<sup>2+</sup>-CaM) binds to the core region of activated STIM1. This interaction facilitates slow Ca<sup>2+</sup>-dependent inactivation after Orai1 channel activation by wild-type STIM1 or a constitutively active STIM1 mutant. We define the CaM-binding site in STIM1, which is adjacent to the STIM1-Orai1 coupling region. The binding of Ca<sup>2+</sup>-CaM to activated STIM1 disrupts the STIM1-Orai1 complex and also disassembles STIM1 oligomer. Based on these results we propose a model for the calcium-bound CaM-regulated deactivation of SOCE.
Medical subject headings
- Calcium
- Calmodulin
- Neoplasm Proteins
- ORAI1 Protein
- Stromal Interaction Molecule 1