Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The third transmembrane segment of orai1 protein modulates Ca2+ release-activated Ca2+ (CRAC) channel gating and permeation properties.

The Journal of biological chemistry - 7 Oct 2011

Srikanth Sonal, Yee Ma-Khin Win, Gwack Yousang, Ribalet Bernard

Abstract excerpt

Orai1, the pore subunit of Ca(2+) release-activated Ca(2+) channels, has four transmembrane segments (TMs). The first segment, TMI, lines the pore and plays an important role in channel activation and ion permeation. TMIII, on the other hand, does not line the pore but still regulates channel gating and permeation properties. To understand the role of TMIII, we have mutated and characterized several residues in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calcium
Share to Calcium Channels

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Calcium Signaling

Share to Cell Membrane

Share to NFATC Transcription Factors

Share to ORAI1 Protein

Share to Patch-Clamp Techniques

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 21865174
DOI: 10.1074/jbc.M111.265884
PMCID: PMC3186358

Genes

STIM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The third transmembrane segment of orai1 protein modulates Ca2+ release-activated Ca2+ (CRAC) channel gating and permeation properties.PMID 21865174Read ↗

Differential roles of the C and N termini of Orai1 protein in interacting with stromal interaction molecule 1 (STIM1) for Ca2+ release-activated Ca2+ (CRAC) channel activation.Semantic proximity Read ↗

Gated regulation of CRAC channel ion selectivity by STIM1.Semantic proximity Read ↗

A single lysine in the N-terminal region of store-operated channels is critical for STIM1-mediated gating.Semantic proximity Read ↗

Orai1 is an essential pore subunit of the CRAC channel.Semantic proximity Read ↗

A Ca2(+ )release-activated Ca2(+) (CRAC) modulatory domain (CMD) within STIM1 mediates fast Ca2(+)-dependent inactivation of ORAI1 channels.Semantic proximity Read ↗

Store-dependent and -independent modes regulating Ca2+ release-activated Ca2+ channel activity of human Orai1 and Orai3.Semantic proximity Read ↗

Dissecting gating mechanisms of Orai calcium channel paralogs using constitutively active Orai mutants that mimic STIM1-gated stateSemantic proximity Read ↗

The inactivation domain of STIM1 is functionally coupled with the Orai1 pore to enable Ca2+-dependent inactivation.Semantic proximity Read ↗

CRAC channel opening is determined by a series of Orai1 gating checkpoints in the transmembrane and cytosolic regions.Semantic proximity Read ↗

STIM1 activates CRAC channels through rotation of the pore helix to open a hydrophobic gate.Semantic proximity Read ↗

2-aminoethoxydiphenyl borate alters selectivity of Orai3 channels by increasing their pore size.Semantic proximity Read ↗

A pathogenic human Orai1 mutation unmasks STIM1-independent rapid inactivation of Orai1 channels.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.