The anatomy of native CRAC channel(s)

Ryan E. Yoast, Scott M. Emrich, Mohamed Trebak

Research output: Contribution to journalReview articlepeer-review

1 Scopus citations

Abstract

The ubiquitous store-operated Ca2+ entry pathway mediated by plasma membrane Ca2+ release-activated Ca2+ (CRAC) channels regulates a wide variety of physiological functions. While it is clearly established that the ORAI1 protein is essential for native mammalian CRAC channels, the contribution of ORAI2 and ORAI3 have remained nebulous. The crystal structure of the sole Orai isoform in drosophila (dOrai) revealed a hexameric assembly, suggesting that mammalian CRAC channels are hexamers of ORAI. Nevertheless, the relative contribution of each isoform of the mammalian ORAI trio to the stoichiometry of native CRAC channels remains elusive. The recent generation of ORAI isoform single, double and triple knockout cell lines and tissue-specific knockout mice has shed light on how native ORAI isoform heteromerization fine tunes CRAC-mediated Ca2+ signaling.

Original languageEnglish (US)
Pages (from-to)89-95
Number of pages7
JournalCurrent Opinion in Physiology
Volume17
DOIs
StatePublished - Oct 2020

All Science Journal Classification (ASJC) codes

  • Physiology
  • Physiology (medical)

Fingerprint Dive into the research topics of 'The anatomy of native CRAC channel(s)'. Together they form a unique fingerprint.

Cite this