Evidence for an interaction between Golli AND STIM1 in store-operated calcium entry

Ciara M Walsh , Mary K Doherty , Alexei V Tepikin , Robert D Burgoyne (1)

1 The Physiological Laboratory

Store operated Ca2+ channels (SOCs) are highly selective ion channels which are activated upon release of Ca2+ from intracellular stores to regulate a multitude of diverse cellular functions. It was recently reported that Golli-BG21, a member of the myelin basic protein (MBP) family of proteins, regulates store operated calcium entry (SOCE) in T-cells and oligodendrocyte precursor cells but the underlying mechanism for this regulation is unknown. Here, we have discovered Golli can directly interact with the ER Ca2+-sensing protein, STIM1. Golli interacts with the C-terminal domain of STIM1 in both in vitro and in vivo binding assays and this interaction may be modulated by intracellular Ca2+ concentration. Golli also colocalises with full length STIM1 and Orai1 complexes in HeLa cells following store depletion. Overexpression of Golli reduces SOCE in HeLa cells but this inhibition is overcome by overexpressing STIM1. We therefore suggest that Golli binds to STIM1-Orai1 complexes to negatively regulate the activity of SOCs.

Mots clés: Life Sciences

Ciara M Walsh, Mary K Doherty, Alexei V Tepikin, Robert D Burgoyne. Evidence for an interaction between Golli AND STIM1 in store-operated calcium entry. Biochemical Journal, 2010, 430 (3), pp.453-460. ⟨10.1042/BJ20100650⟩. ⟨hal-00512011⟩