Ontology highlight
ABSTRACT:
SUBMITTER: Yamashita M
PROVIDER: S-EPMC5321763 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Yamashita Megumi M Yeung Priscilla S-W PS Ing Christopher E CE McNally Beth A BA Pomès Régis R Prakriya Murali M
Nature communications 20170221
Store-operated Ca<sup>2+</sup> release-activated Ca<sup>2+</sup> (CRAC) channels constitute a major pathway for Ca<sup>2+</sup> influx and mediate many essential signalling functions in animal cells, yet how they open remains elusive. Here, we investigate the gating mechanism of the human CRAC channel Orai1 by its activator, stromal interacting molecule 1 (STIM1). We find that two rings of pore-lining residues, V102 and F99, work together to form a hydrophobic gate. Mutations of these residues t ...[more]