An open pore structure of the Orai channel, finally

Murali Prakriya; Priscilla See-Wai Yeung; Megumi Yamashita

doi:10.1016/j.ceca.2021.102366

An open pore structure of the Orai channel, finally

Cell Calcium. 2021 Mar:94:102366. doi: 10.1016/j.ceca.2021.102366. Epub 2021 Feb 2.

Authors

Murali Prakriya¹, Priscilla See-Wai Yeung², Megumi Yamashita²

Affiliations

¹ Department of Pharmacology, Northwestern University, Feinberg School of Medicine, Chicago, IL, 60611, United States. Electronic address: m-prakriya@northwestern.edu.
² Department of Pharmacology, Northwestern University, Feinberg School of Medicine, Chicago, IL, 60611, United States.

Abstract

Store-operated Orai channels are a primary mechanism for mobilizing Ca²⁺ signals in both non-excitable cells and excitable cells. The structure of the open channel, vital for understanding the mechanism of channel opening, is incompletely understood. We highlight a new study that unveils the structure of a constitutively active Orai mutant and takes us closer towards understanding the molecular basis of Orai channel activation.

Keywords: Calcium selectivity; Ion channel; Ion channel gating; Orai; Orai1; STIM1; Structure.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Animals
Drosophila melanogaster / metabolism
Humans
Hydrophobic and Hydrophilic Interactions
Ion Channel Gating
ORAI1 Protein / chemistry
ORAI1 Protein / metabolism*
ORAI1 Protein / ultrastructure
Protein Conformation

Substances

ORAI1 Protein

Grants and funding

R01 NS057499/NS/NINDS NIH HHS/United States