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

Interaction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling.

Proceedings of the National Academy of Sciences of the United States of America - 27 Dec 2005

Cheng Weijun, Altafaj Xavier, Ronjat Michel, Coronado Roberto

Abstract excerpt

Previous studies have shown that the skeletal dihydropyridine receptor (DHPR) pore subunit Ca(V)1.1 (alpha1S) physically interacts with ryanodine receptor type 1 (RyR1), and a molecular signal is transmitted from alpha1S to RyR1 to trigger excitation-contraction (EC) coupling. We show that the beta-subunit of the skeletal DHPR also binds RyR1 and participates in this signaling process. A novel binding site for...

Read the complete abstract on PubMed

Topics

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

Share to Bone and Bones
Share to Calcium Channels

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

Share to Calcium Channels, L-Type

Share to Caveolin 1

Share to Muscles

Share to Patch-Clamp Techniques

Share to Ryanodine Receptor Calcium Release Channel

Share to Sarcoplasmic Reticulum

Source

Open in PubMed Open full text

Identifiers

PMID: 16357209
DOI: 10.1073/pnas.0504334102
PMCID: PMC1323149

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

Interaction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling.PMID 16357209Read ↗

Ca2+-dependent excitation-contraction coupling triggered by the heterologous cardiac/brain DHPR beta2a-subunit in skeletal myotubes.Semantic proximity Read ↗

A component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the dihydropyridine receptor alpha(1s) pore subunit.Semantic proximity Read ↗

RyR1-mediated Ca2+-induced Ca2+ release plays a negligible role in excitation-contraction coupling of normal skeletal muscle.Semantic proximity Read ↗

Multiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle.Semantic proximity Read ↗

Dihydropyridine receptor (DHPR, CACNA1S) congenital myopathy.Semantic proximity Read ↗

Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: size and charge do matter.Semantic proximity Read ↗

Ca2+ handling abnormalities in early-onset muscle diseases: Novel concepts and perspectives.Semantic proximity Read ↗

Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion.Semantic proximity Read ↗

Structure and Function of the Human Ryanodine Receptors and Their Association with Myopathies—Present State, Challenges, and PerspectivesSemantic proximity Read ↗

RyR1 deficiency in congenital myopathies disrupts excitation-contraction coupling.Semantic proximity Read ↗

Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.Semantic proximity Read ↗

Cardiac-type EC-coupling in dysgenic myotubes restored with Ca2+ channel subunit isoforms alpha1C and alpha1D does not correlate with current density.Semantic proximity Read ↗

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