Amino Acid Residues 489–503 of Dihydropyridine Receptor (DHPR) β1a Subunit Are Critical for Structural Communication between the Skeletal Muscle DHPR Complex and Type 1 Ryanodine Receptor
José M. Eltit; Clara Franzini‐Armstrong; Claudio F. Pérez · 2014 · Journal of Biological Chemistry
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Abstract
The β1a subunit is a cytoplasmic component of the dihydropyridine receptor (DHPR) complex that plays an essential role in skeletal muscle excitation-contraction (EC) coupling. Here we investigate the role of the C-terminal end of this auxiliary subunit in the functional and structural communication between the DHPR and the Ca2+ release channel (RyR1). Progressive truncation of the β1a C terminus showed that deletion of amino acid residues Gln489 to Trp503 resulted in a loss of depolarization-induced Ca2+ release, a severe reduction of L-type Ca2+ currents, and a lack of tetrad formation as eva
Abstract by José M. Eltit; Clara Franzini‐Armstrong; Claudio F. Pérez, Journal of Biological Chemistry (2014) — licensed CC BY 4.0.
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Metadata source: OpenAlex · DOI 10.1074/jbc.m114.615526