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An alpha-helical C-terminal tail segment of the skeletal L-type Ca2+ channel beta1a subunit activates ryanodine receptor type 1 via a hydrophobic surface

Karunasekara, Yamuna; Rebbeck, Robyn; Weaver, Llara; Board, Philip; Dulhunty, Angela; Casarotto, Marco


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 β1a subunit adopt a nascent α-helix in which 3 hydrophobic residues align to form a hydrophobic surface that binds to RyR1 isolated from rabbit skeletal muscle. Mutation of the hydrophobic...[Show more]

CollectionsANU Research Publications
Date published: 2012
Type: Journal article
Source: FASEB Journal
DOI: 10.1096/fj.12-211334


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