STIM1 activates CRAC channels through rotation of the pore helix to open a hydrophobic gate

Megumi Yamashita; Priscilla S.-W. Yeung; Christopher E. Ing; Beth A. McNally; Régis Pomès; Murali Prakriya

doi:10.1038/ncomms14512

Nature Communications (Feb 2017)

STIM1 activates CRAC channels through rotation of the pore helix to open a hydrophobic gate

Megumi Yamashita,
Priscilla S.-W. Yeung,
Christopher E. Ing,
Beth A. McNally,
Régis Pomès,
Murali Prakriya

Affiliations

Megumi Yamashita: Department of Pharmacology, Feinberg School of Medicine, Northwestern University
Priscilla S.-W. Yeung: Department of Pharmacology, Feinberg School of Medicine, Northwestern University
Christopher E. Ing: Molecular Structure and Function, Hospital for Sick Children, University of Toronto
Beth A. McNally: Department of Pharmacology, Feinberg School of Medicine, Northwestern University
Régis Pomès: Molecular Structure and Function, Hospital for Sick Children, University of Toronto
Murali Prakriya: Department of Pharmacology, Feinberg School of Medicine, Northwestern University

DOI: https://doi.org/10.1038/ncomms14512
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

Read online

Store-operated Ca2+channels (CRAC) are involved in several cellular functions. Here the authors identify a hydrophobic gate in the CRAC pore and show that CRAC activation by STIM1 involves rotation of the pore helix that hydrates this region to allow ion passage through the pore.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal