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Article

STAC3 binding to CaV1.1 II-III loop is nonessential but critically supports skeletal muscle excitation-contraction coupling.

JCI insight - 8 Aug 2025

Tuinte Wietske E, Török Enikő, Tuluc Petronel, Fattori Fabiana, D'Amico Adele, Campiglio Marta

Abstract excerpt

Skeletal muscle excitation-contraction (EC) coupling depends on the direct coupling between CaV1.1 on the sarcolemma and ryanodine receptor (RyR1) on the sarcoplasmic reticulum. A key regulator of this process is STAC3, a protein essential for both the functional expression of CaV1.1 and its conformational coupling with RyR1. Mutations in Stac3 cause STAC3 disorder, a congenital myopathy characterized by muscle...

Read the complete abstract on PubMed

Topics

Humans
Muscle, Skeletal
Excitation Contraction Coupling
Ryanodine Receptor Calcium Release Channel
Calcium Channels, L-Type

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

Animals

Mutation

Protein Binding

Mice

Caveolin 1

Source

Open in PubMed Open full text

Identifiers

PMID: 40779452
DOI: 10.1172/jci.insight.191053
PMCID: PMC12333939

Genes

STAC3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 19 Oct 2026.

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STAC3 binding to CaV1.1 II-III loop is nonessential but critically supports skeletal muscle excitation-contraction coupling.PMID 40779452Read ↗

Structural insights into binding of STAC proteins to voltage-gated calcium channels.Semantic proximity Read ↗

Stac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation.Semantic proximity Read ↗

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Congenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.Semantic proximity Read ↗

STAC3 variants cause a congenital myopathy with distinctive dysmorphic features and malignant hyperthermia susceptibility.Semantic proximity Read ↗

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