Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation.

ABSTRACT: The calcium release activated calcium channel is activated by the endoplasmic reticulum-resident calcium sensor protein STIM1. On activation, STIM1 C terminus changes from an inactive, tight to an active, extended conformation. A coiled-coil clamp involving the CC1 and CC3 domains is essential in controlling STIM1 activation, with CC1 as the key entity. The nuclear magnetic resonance-derived solution structure of the CC1 domain represents a three-helix bundle stabilized by interhelical contacts, which are absent in the Stormorken disease-related STIM1 R304W mutant. Two interhelical sites between the CC1α₁ and CC1α₂ helices are key in controlling STIM1 activation, affecting the balance between tight and extended conformations. Nuclear magnetic resonance-directed mutati

SUBMITTER: Rathner P 

PROVIDER: S-EPMC7610458 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature