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Article

An α-helical C-terminal tail segment of the skeletal L-type Ca2+ channel β1a subunit activates ryanodine receptor type 1 via a hydrophobic surface.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Dec 2012

Karunasekara Yamuna, Rebbeck Robyn T, Weaver Llara M, Board Philip G, Dulhunty Angela F, Casarotto Marco G

Abstract excerpt

Excitation-contraction (EC) coupling in skeletal muscle depends on protein interactions between the transverse tubule dihydropyridine receptor (DHPR) voltage sensor and intracellular ryanodine receptor (RyR1) calcium release channel. We present novel data showing that the C-terminal 35 residues of the β(1a) subunit adopt a nascent α-helix in which 3 hydrophobic residues align to form a hydrophobic surface that...

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Identifiers

PMID: 22962299
DOI: 10.1096/fj.12-211334

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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An α-helical C-terminal tail segment of the skeletal L-type Ca2+ channel β1a subunit activates ryanodine receptor type 1 via a hydrophobic surface.PMID 22962299Read ↗

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

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

Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors.Semantic proximity Read ↗

The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule.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 ↗

Domain cooperativity in the β1a subunit is essential for dihydropyridine receptor voltage sensing in 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 ↗

A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor.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 ↗

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Structural and functional interactions between the EF hand domain and S2-S3 loop in the type-1 ryanodine receptor ion channel.Semantic proximity Read ↗

Structural determination of the phosphorylation domain of the ryanodine receptor.Semantic proximity Read ↗

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