Functional characterization of the type 1 inositol 1,4,5-trisphosphate receptor coupling domain SII(+/-) splice variants and the Opisthotonos mutant form.

doi:10.1016/S0006-3495(02)75548-3

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Article

Functional characterization of the type 1 inositol 1,4,5-trisphosphate receptor coupling domain SII(+/-) splice variants and the Opisthotonos mutant form.

Biophysical journal - 1 Apr 2002

Tu Huiping, Miyakawa Tomoya, Wang Zhengnan, Glouchankova Lyuba, Iino Masamitsu, Bezprozvanny Ilya

Abstract excerpt

The type 1 inositol (1,4,5)-trisphosphate receptor (InsP3R1) plays a critical role in Ca2+ signaling in cells. Neuronal and nonneuronal isoforms of the InsP3R1 differ by alternative splicing in the coupling domain of the InsP3R1 (SII site). Deletion of 107 amino acids from the coupling domain of...

Topics

Adenosine Triphosphate
Allosteric Site
Alternative Splicing
Animals
Calcium
Calcium Channels
Cell Line
Chickens
Cytosol
Electrophysiology
Inositol 1,4,5-Trisphosphate Receptors
Insecta
Mice
Microsomes
Models, Genetic

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Identifiers

PMID: 11916857
DOI: 10.1016/S0006-3495(02)75548-3
PMCID: PMC1301995

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-11916857-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Mutation

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Protein Structure, Tertiary