title: Postulated role of inter-domain interaction within the ryanodine receptor in Ca(2+) channel regulation.
abstract: Key steps of excitation-contraction (E-C) coupling are (1) binding of the activator portion of the dihydropyridine (DHP) receptor (in skeletal muscle) or binding of the Ca(2+) entered through the DHP receptor (in cardiac muscle) to the ryanodine receptor (RyR), (2) a global protein conformational change of the RyR, and (3) opening of the RyR Ca(2+) channel, leading to muscle contraction. The conformational change (step 2) plays a major role in the Ca(2+) channel regulation, and a number of "regulatory domains" must be involved in this process. We postulate that the interaction among these regulatory domains is the central mechanism for the conformation-mediated control of the Ca(2+) channel. In this review, we summarize the recent data supporting this concept.
authors.affiliation: Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA. ikemoto@bbri.org
authors.forename: N
authors.initials: N
authors.lastname: Ikemoto
authors.forename: T
authors.initials: T
authors.lastname: Yamamoto
mesh_terms: D015220:Calcium Channels / Q000235:genetics*; D005786:Gene Expression Regulation; D006801:Humans; D017434:Protein Structure, Tertiary / Q000502:physiology; D019837:Ryanodine Receptor Calcium Release Channel / Q000502:physiology*
chemical_list: D015220:Calcium Channels; D019837:Ryanodine Receptor Calcium Release Channel